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This is a searchable collection of scientific photos, illustrations, and videos. The images and videos in this gallery are licensed under Creative Commons Attribution Non-Commercial ShareAlike 3.0. This license lets you remix, tweak, and build upon this work non-commercially, as long as you credit and license your new creations under identical terms.
2841: Circadian rhythm
2841: Circadian rhythm
The human body keeps time with a master clock called the suprachiasmatic nucleus or SCN. Situated inside the brain, it's a tiny sliver of tissue about the size of a grain of rice, located behind the eyes. It sits quite close to the optic nerve, which controls vision, and this means that the SCN "clock" can keep track of day and night. The SCN helps control sleep by coordinating the actions of billions of miniature "clocks" throughout the body. These aren't actually clocks, but rather are ensembles of genes inside clusters of cells that switch on and off in a regular, 24-hour cycle in our physiological day.
Crabtree + Company
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3254: Pulsating response to stress in bacteria - video
3254: Pulsating response to stress in bacteria - video
By attaching fluorescent proteins to the genetic circuit responsible for B. subtilis's stress response, researchers can observe the cells' pulses as green flashes. This video shows flashing cells as they multiply over the course of more than 12 hours. In response to a stressful environment like one lacking food, B. subtilis activates a large set of genes that help it respond to the hardship. Instead of leaving those genes on as previously thought, researchers discovered that the bacteria flip the genes on and off, increasing the frequency of these pulses with increasing stress. See entry 3253 for a related still image.
Michael Elowitz, Caltech University
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1011: Lily mitosis 11
1011: Lily mitosis 11
A light microscope image of cells from the endosperm of an African globe lily (Scadoxus katherinae). This is one frame of a time-lapse sequence that shows cell division in action. The lily is considered a good organism for studying cell division because its chromosomes are much thicker and easier to see than human ones. Staining shows microtubules in red and chromosomes in blue. Here, condensed chromosomes are clearly visible and have separated into the opposite sides of a dividing cell.
Related to images 1010, 1012, 1013, 1014, 1015, 1016, 1017, 1018, 1019, and 1021.
Related to images 1010, 1012, 1013, 1014, 1015, 1016, 1017, 1018, 1019, and 1021.
Andrew S. Bajer, University of Oregon, Eugene
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2317: Fruitful dyes
2317: Fruitful dyes
These colorful, computer-generated ribbons show the backbone of a molecule that glows a fluorescent red. The molecule, called mStrawberry, was created by chemists based on a protein found in the ruddy lips of a coral. Scientists use the synthetic molecule and other "fruity" ones like it as a dye to mark and study cell structures.
Roger Y. Tsien, University of California, San Diego
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3727: Zinc levels in a plant leaf
3727: Zinc levels in a plant leaf
Zinc is required for the function of more than 300 enzymes, including those that help regulate gene expression, in various organisms including humans. Researchers study how plants acquire, sequester and distribute zinc to find ways to increase the zinc content of crops to improve human health. Using synchrotron X-ray fluorescence technology, they created this heat map of zinc levels in an Arabidopsis thaliana plant leaf. This image is a winner of the 2015 FASEB Bioart contest and was featured in the NIH Director's blog.
Suzana Car, Dartmouth College
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5768: Multivesicular bodies containing intralumenal vesicles assemble at the vacuole 2
5768: Multivesicular bodies containing intralumenal vesicles assemble at the vacuole 2
Collecting and transporting cellular waste and sorting it into recylable and nonrecylable pieces is a complex business in the cell. One key player in that process is the endosome, which helps collect, sort and transport worn-out or leftover proteins with the help of a protein assembly called the endosomal sorting complexes for transport (or ESCRT for short). These complexes help package proteins marked for breakdown into intralumenal vesicles, which, in turn, are enclosed in multivesicular bodies for transport to the places where the proteins are recycled or dumped. In this image, a multivesicular body (the round structure slightly to the right of center) contain tiny intralumenal vesicles (with a diameter of only 25 nanometers; the round specks inside the larger round structure) adjacent to the cell's vacuole (below the multivesicular body, shown in darker and more uniform gray).
Scientists working with baker's yeast (Saccharomyces cerevisiae) study the budding inward of the limiting membrane (green lines on top of the yellow lines) into the intralumenal vesicles. This tomogram was shot with a Tecnai F-20 high-energy electron microscope, at 29,000x magnification, with a 0.7-nm pixel, ~4-nm resolution.
To learn more about endosomes, see the Biomedical Beat blog post The Cell’s Mailroom. Related to a color-enhanced version 5767 and image 5769.
Scientists working with baker's yeast (Saccharomyces cerevisiae) study the budding inward of the limiting membrane (green lines on top of the yellow lines) into the intralumenal vesicles. This tomogram was shot with a Tecnai F-20 high-energy electron microscope, at 29,000x magnification, with a 0.7-nm pixel, ~4-nm resolution.
To learn more about endosomes, see the Biomedical Beat blog post The Cell’s Mailroom. Related to a color-enhanced version 5767 and image 5769.
Matthew West and Greg Odorizzi, University of Colorado
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3648: Symmetrically and asymmetrically elongating cells
3648: Symmetrically and asymmetrically elongating cells
Merged fluorescent images of symmetrically (left) or asymmetrically (right) elongating HeLa cells at the end of early anaphase (magenta) and late anaphase (green). Chromosomes and cortical actin are visualized by expressing mCherry-histone H2B and Lifeact-mCherry. Scale bar, 10µm. See the PubMed abstract of this research.
Tomomi Kiyomitsu and Iain M. Cheeseman, Whitehead Institute for Biomedical Research
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6984: Fruit fly starvation leads to adipokine accumulation
6984: Fruit fly starvation leads to adipokine accumulation
Adult Drosophila abdominal fat tissue showing cell nuclei labelled in magenta. The upper panel is from well-fed flies, and the lower panel is from flies that have been deprived of food for 4 hours. Starvation results in the accumulation of a key adipokine—a fat hormone (blue-green dots).
Related to images 6982, 6983, and 6985.
Related to images 6982, 6983, and 6985.
Akhila Rajan, Fred Hutchinson Cancer Center
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2554: RNA strand
2554: RNA strand
Ribonucleic acid (RNA) has a sugar-phosphate backbone and the bases adenine (A), cytosine (C), guanine (G), and uracil (U). See image 2555 for a labeled version of this illustration. Featured in The New Genetics.
Crabtree + Company
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3550: Protein clumping in zinc-deficient yeast cells
3550: Protein clumping in zinc-deficient yeast cells
The green spots in this image are clumps of protein inside yeast cells that are deficient in both zinc and a protein called Tsa1 that prevents clumping. Protein clumping plays a role in many diseases, including Parkinson's and Alzheimer's, where proteins clump together in the brain. Zinc deficiency within a cell can cause proteins to mis-fold and eventually clump together. Normally, in yeast, Tsa1 codes for so-called "chaperone proteins" which help proteins in stressed cells, such as those with a zinc deficiency, fold correctly. The research behind this image was published in 2013 in the Journal of Biological Chemistry.
Colin MacDiarmid and David Eide, University of Wisconsin--Madison
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5895: Bioluminescence in a Tube
5895: Bioluminescence in a Tube
Details about the basic biology and chemistry of the ingredients that produce bioluminescence are allowing scientists to harness it as an imaging tool. Credit: Nathan Shaner, Scintillon Institute.
From Biomedical Beat article July 2017: Chasing Fireflies—and Better Cellular Imaging Techniques
From Biomedical Beat article July 2017: Chasing Fireflies—and Better Cellular Imaging Techniques
Nathan Shaner, Scintillon Institute
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6934: Zebrafish head vasculature
6934: Zebrafish head vasculature
A zebrafish head with blood vessels shown in purple. Researchers often study zebrafish because they share many genes with humans, grow and reproduce quickly, and have see-through eggs and embryos, which make it easy to study early stages of development.
This image was captured using a light sheet microscope.
Related to video 6933.
This image was captured using a light sheet microscope.
Related to video 6933.
Prayag Murawala, MDI Biological Laboratory and Hannover Medical School.
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3287: Retinal pigment epithelium derived from human ES cells 02
3287: Retinal pigment epithelium derived from human ES cells 02
This image shows a layer of retinal pigment epithelium cells derived from human embryonic stem cells, highlighting the nuclei (red) and cell surfaces (green). This kind of retinal cell is responsible for macular degeneration, the most common cause of blindness. Image and caption information courtesy of the California Institute for Regenerative Medicine. Related to image 3286
David Buckholz and Sherry Hikita, University of California, Santa Barbara, via CIRM
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3786: Movie of in vitro assembly of a cell-signaling pathway
3786: Movie of in vitro assembly of a cell-signaling pathway
T cells are white blood cells that are important in defending the body against bacteria, viruses and other pathogens. Each T cell carries proteins, called T-cell receptors, on its surface that are activated when they come in contact with an invader. This activation sets in motion a cascade of biochemical changes inside the T cell to mount a defense against the invasion. Scientists have been interested for some time what happens after a T-cell receptor is activated. One obstacle has been to study how this signaling cascade, or pathway, proceeds inside T cells.
In this video, researchers have created a T-cell receptor pathway consisting of 12 proteins outside the cell on an artificial membrane. The video shows three key steps during the signaling process: phosphorylation of the T-cell receptor (green), clustering of a protein called linker for activation of T cells (LAT) (blue) and polymerization of the cytoskeleton protein actin (red). The findings show that the T-cell receptor signaling proteins self-organize into separate physical and biochemical compartments. This new system of studying molecular pathways outside the cells will enable scientists to better understand how the immune system combats microbes or other agents that cause infection.
To learn more how researchers assembled this T-cell receptor pathway, see this press release from HHMI's Marine Biological Laboratory Whitman Center. Related to image 3787.
In this video, researchers have created a T-cell receptor pathway consisting of 12 proteins outside the cell on an artificial membrane. The video shows three key steps during the signaling process: phosphorylation of the T-cell receptor (green), clustering of a protein called linker for activation of T cells (LAT) (blue) and polymerization of the cytoskeleton protein actin (red). The findings show that the T-cell receptor signaling proteins self-organize into separate physical and biochemical compartments. This new system of studying molecular pathways outside the cells will enable scientists to better understand how the immune system combats microbes or other agents that cause infection.
To learn more how researchers assembled this T-cell receptor pathway, see this press release from HHMI's Marine Biological Laboratory Whitman Center. Related to image 3787.
Xiaolei Su, HHMI Whitman Center of the Marine Biological Laboratory
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3613: Abnormal, spiky fibroblast
3613: Abnormal, spiky fibroblast
This is a fibroblast, a connective tissue cell that plays an important role in wound healing. Normal fibroblasts have smooth edges. In contrast, this spiky cell is missing a protein that is necessary for proper construction of the cell's skeleton. Its jagged shape makes it impossible for the cell to move normally. In addition to compromising wound healing, abnormal cell movement can lead to birth defects, faulty immune function, and other health problems.
This image was part of the Life: Magnified exhibit that ran from June 3, 2014, to January 21, 2015, at Dulles International Airport.
This image was part of the Life: Magnified exhibit that ran from June 3, 2014, to January 21, 2015, at Dulles International Airport.
Praveen Suraneni, Stowers Institute for Medical Research, Kansas City, Mo.
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6963: C. elegans trapped by carnivorous fungus
6963: C. elegans trapped by carnivorous fungus
Real-time footage of Caenorhabditis elegans, a tiny roundworm, trapped by a carnivorous fungus, Arthrobotrys dactyloides. This fungus makes ring traps in response to the presence of C. elegans. When a worm enters a ring, the trap rapidly constricts so that the worm cannot move away, and the fungus then consumes the worm. The size of the imaged area is 0.7mm x 0.9mm.
This video was obtained with a polychromatic polarizing microscope (PPM) in white light that shows the polychromatic birefringent image with hue corresponding to the slow axis orientation. More information about PPM can be found in the Scientific Reports paper “Polychromatic Polarization Microscope: Bringing Colors to a Colorless World” by Shribak.
This video was obtained with a polychromatic polarizing microscope (PPM) in white light that shows the polychromatic birefringent image with hue corresponding to the slow axis orientation. More information about PPM can be found in the Scientific Reports paper “Polychromatic Polarization Microscope: Bringing Colors to a Colorless World” by Shribak.
Michael Shribak, Marine Biological Laboratory/University of Chicago.
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3486: Apoptosis reversed
3486: Apoptosis reversed
Two healthy cells (bottom, left) enter into apoptosis (bottom, center) but spring back to life after a fatal toxin is removed (bottom, right; top).
Hogan Tang of the Denise Montell Lab, Johns Hopkins University School of Medicine
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3403: Disrupted vascular development in frog embryos
3403: Disrupted vascular development in frog embryos
Disassembly of vasculature in kdr:GFP frogs following addition of 250 µM TBZ. Related to images 3404 and 3505.
Hye Ji Cha, University of Texas at Austin
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5857: 3D reconstruction of a tubular matrix in peripheral endoplasmic reticulum
5857: 3D reconstruction of a tubular matrix in peripheral endoplasmic reticulum
Detailed three-dimensional reconstruction of a tubular matrix in a thin section of the peripheral endoplasmic reticulum between the plasma membranes of the cell. The endoplasmic reticulum (ER) is a continuous membrane that extends like a net from the envelope of the nucleus outward to the cell membrane. The ER plays several roles within the cell, such as in protein and lipid synthesis and transport of materials between organelles. Shown here is a three-dimensional representation of the peripheral ER microtubules. Related to images 5855 and 5856
Jennifer Lippincott-Schwartz, Howard Hughes Medical Institute Janelia Research Campus, Virginia
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2594: Katanin protein regulates anaphase
2594: Katanin protein regulates anaphase
The microtubule severing protein, katanin, localizes to chromosomes and regulates anaphase A in mitosis. The movement of chromosomes on the mitotic spindle requires the depolymerization of microtubule ends. The figure shows the mitotic localization of the microtubule severing protein katanin (green) relative to spindle microtubules (red) and kinetochores/chromosomes (blue). Katanin targets to chromosomes during both metaphase (top) and anaphase (bottom) and is responsible for inducing the depolymerization of attached microtubule plus-ends. This image was a finalist in the 2008 Drosophila Image Award.
David Sharp, Albert Einstein College of Medicine
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6581: Fluorescent C. elegans showing muscle and ribosomal protein
6581: Fluorescent C. elegans showing muscle and ribosomal protein
C. elegans, a tiny roundworm, with a ribosomal protein glowing red and muscle fibers glowing green. Researchers used these worms to study a molecular pathway that affects aging. The ribosomal protein is involved in protein translation and may play a role in dietary restriction-induced longevity. Image created using confocal microscopy.
View group of roundworms here 6582.
View closeup of roundworms here 6583.
View group of roundworms here 6582.
View closeup of roundworms here 6583.
Jarod Rollins, Mount Desert Island Biological Laboratory.
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6748: Human retinal organoid
6748: Human retinal organoid
A replica of a human retina grown from stem cells. It shows rod photoreceptors (nerve cells responsible for dark vision) in green and red/green cones (nerve cells responsible for red and green color vision) in red. The cell nuclei are stained blue. This image was captured using a confocal microscope.
Kevin Eliceiri, University of Wisconsin-Madison.
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3732: A molecular interaction network in yeast 2
3732: A molecular interaction network in yeast 2
The image visualizes a part of the yeast molecular interaction network. The lines in the network represent connections among genes (shown as little dots) and different-colored networks indicate subnetworks, for instance, those in specific locations or pathways in the cell. Researchers use gene or protein expression data to build these networks; the network shown here was visualized with a program called Cytoscape. By following changes in the architectures of these networks in response to altered environmental conditions, scientists can home in on those genes that become central "hubs" (highly connected genes), for example, when a cell encounters stress. They can then further investigate the precise role of these genes to uncover how a cell's molecular machinery deals with stress or other factors. Related to images 3730 and 3733.
Keiichiro Ono, UCSD
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6346: Intasome
6346: Intasome
Salk researchers captured the structure of a protein complex called an intasome (center) that lets viruses similar to HIV establish permanent infection in their hosts. The intasome hijacks host genomic material, DNA (white) and histones (beige), and irreversibly inserts viral DNA (blue). The image was created by Jamie Simon and Dmitry Lyumkis. Work that led to the 3D map was published in: Ballandras-Colas A, Brown M, Cook NJ, Dewdney TG, Demeler B, Cherepanov P, Lyumkis D, & Engelman AN. (2016). Cryo-EM reveals a novel octameric integrase structure for ?-retroviral intasome function. Nature, 530(7590), 358—361
National Resource for Automated Molecular Microscopy http://nramm.nysbc.org/nramm-images/ Source: Bridget Carragher
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3274: Human embryonic stem cells on feeder cells
3274: Human embryonic stem cells on feeder cells
This fluorescent microscope image shows human embryonic stem cells whose nuclei are stained green. Blue staining shows the surrounding supportive feeder cells. Image and caption information courtesy of the California Institute for Regenerative Medicine. See related image 3275.
Michael Longaker lab, Stanford University School of Medicine, via CIRM
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3429: Enzyme transition states
3429: Enzyme transition states
The molecule on the left is an electrostatic potential map of the van der Waals surface of the transition state for human purine nucleoside phosphorylase. The colors indicate the electron density at any position of the molecule. Red indicates electron-rich regions with negative charge and blue indicates electron-poor regions with positive charge. The molecule on the right is called DADMe-ImmH. It is a chemically stable analogue of the transition state on the left. It binds to the enzyme millions of times tighter than the substrate. This inhibitor is in human clinical trials for treating patients with gout. This image appears in Figure 4, Schramm, V.L. (2011) Annu. Rev. Biochem. 80:703-732.
Vern Schramm, Albert Einstein College of Medicine of Yeshiva University
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6547: Cell Nucleus and Lipid Droplets
6547: Cell Nucleus and Lipid Droplets
A cell nucleus (blue) surrounded by lipid droplets (yellow). Exogenously expressed, S-tagged UBXD8 (green) recruits endogenous p97/VCP (red) to the surface of lipid droplets in oleate-treated HeLa cells. Nucleus stained with DAPI.
James Olzmann, University of California, Berkeley
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2715: Glow-in-the-dark salamanders
2715: Glow-in-the-dark salamanders
These six-month-old axolotls, a kind of salamander, glow green and blue under ultraviolet light. That's because they were genetically modified to make harmless green fluorescent protein, or GFP. Like X-ray vision, GFP lets you see inside the axolotls as they hang out in their aquarium. GFP not only can reveal internal structures in living organisms, but it also can light up specific cells and even proteins within a cell. That allows scientists to identify and track things like cancer cells.
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3492: Glowing bacteria make a pretty postcard
3492: Glowing bacteria make a pretty postcard
This tropical scene, reminiscent of a postcard from Key West, is actually a petri dish containing an artistic arrangement of genetically engineered bacteria. The image showcases eight of the fluorescent proteins created in the laboratory of the late Roger Y. Tsien, a cell biologist at the University of California, San Diego. Tsien, along with Osamu Shimomura of the Marine Biology Laboratory and Martin Chalfie of Columbia University, share the 2008 Nobel Prize in chemistry for their work on green fluorescent protein-a naturally glowing molecule from jellyfish that has become a powerful tool for studying molecules inside living cells.
Nathan C. Shaner, The Scintillon Institute
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3418: X-ray co-crystal structure of Src kinase bound to a DNA-templated macrocycle inhibitor 6
3418: X-ray co-crystal structure of Src kinase bound to a DNA-templated macrocycle inhibitor 6
X-ray co-crystal structure of Src kinase bound to a DNA-templated macrocycle inhibitor. Related to images 3413, 3414, 3415, 3416, 3417, and 3419.
Markus A. Seeliger, Stony Brook University Medical School and David R. Liu, Harvard University
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5751: Genetically identical mycobacteria respond differently to antibiotic 1
5751: Genetically identical mycobacteria respond differently to antibiotic 1
Antibiotic resistance in microbes is a serious health concern. So researchers have turned their attention to how bacteria undo the action of some antibiotics. Here, scientists set out to find the conditions that help individual bacterial cells survive in the presence of the antibiotic rifampicin. The research team used Mycobacterium smegmatis, a more harmless relative of Mycobacterium tuberculosis, which infects the lung and other organs and causes serious disease.
In this image, genetically identical mycobacteria are growing in a miniature growth chamber called a microfluidic chamber. Using live imaging, the researchers found that individual mycobacteria will respond differently to the antibiotic, depending on the growth stage and other timing factors. The researchers used genetic tagging with green fluorescent protein to distinguish cells that can resist rifampicin and those that cannot. With this gene tag, cells tolerant of the antibiotic light up in green and those that are susceptible in violet, enabling the team to monitor the cells' responses in real time.
To learn more about how the researchers studied antibiotic resistance in mycobacteria, see this news release from Tufts University. Related to video 5752.
In this image, genetically identical mycobacteria are growing in a miniature growth chamber called a microfluidic chamber. Using live imaging, the researchers found that individual mycobacteria will respond differently to the antibiotic, depending on the growth stage and other timing factors. The researchers used genetic tagging with green fluorescent protein to distinguish cells that can resist rifampicin and those that cannot. With this gene tag, cells tolerant of the antibiotic light up in green and those that are susceptible in violet, enabling the team to monitor the cells' responses in real time.
To learn more about how the researchers studied antibiotic resistance in mycobacteria, see this news release from Tufts University. Related to video 5752.
Bree Aldridge, Tufts University
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2690: Dolly the sheep
2690: Dolly the sheep
Scientists in Scotland were the first to clone an animal, this sheep named Dolly. She later gave birth to Bonnie, the lamb next to her.
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1013: Lily mitosis 03
1013: Lily mitosis 03
A light microscope image of a cell from the endosperm of an African globe lily (Scadoxus katherinae). This is one frame of a time-lapse sequence that shows cell division in action. The lily is considered a good organism for studying cell division because its chromosomes are much thicker and easier to see than human ones. Staining shows microtubules in red and chromosomes in blue.
Related to images 1010, 1011, 1012, 1014, 1015, 1016, 1017, 1018, 1019, and 1021.
Related to images 1010, 1011, 1012, 1014, 1015, 1016, 1017, 1018, 1019, and 1021.
Andrew S. Bajer, University of Oregon, Eugene
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2332: Tiny points of light in a quantum dot
2332: Tiny points of light in a quantum dot
This fingertip-shaped group of lights is a microscopic crystal called a quantum dot. About 10,000 times thinner than a sheet of paper, the dot radiates brilliant colors under ultraviolet light. Dots such as this one allow researchers to label and track individual molecules in living cells and may be used for speedy disease diagnosis, DNA testing, and screening for illegal drugs.
Sandra Rosenthal and James McBride, Vanderbilt University, and Stephen Pennycook, Oak Ridge National Laboratory
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5761: A panorama view of cells
5761: A panorama view of cells
This photograph shows a panoramic view of HeLa cells, a cell line many researchers use to study a large variety of important research questions. The cells' nuclei containing the DNA are stained in blue and the cells' cytoskeletons in gray.
Tom Deerinck, National Center for Microscopy and Imaging Research
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6556: Floral pattern in a mixture of two bacterial species, Acinetobacter baylyi and Escherichia coli, grown on a semi-solid agar for 72 hour
6556: Floral pattern in a mixture of two bacterial species, Acinetobacter baylyi and Escherichia coli, grown on a semi-solid agar for 72 hour
Floral pattern emerging as two bacterial species, motile Acinetobacter baylyi and non-motile Escherichia coli (green), are grown together for 72 hours on 0.5% agar surface from a small inoculum in the center of a Petri dish.
See 6557 for a photo of this process at 24 hours on 0.75% agar surface.
See 6553 for a photo of this process at 48 hours on 1% agar surface.
See 6555 for another photo of this process at 48 hours on 1% agar surface.
See 6550 for a video of this process.
See 6557 for a photo of this process at 24 hours on 0.75% agar surface.
See 6553 for a photo of this process at 48 hours on 1% agar surface.
See 6555 for another photo of this process at 48 hours on 1% agar surface.
See 6550 for a video of this process.
L. Xiong et al, eLife 2020;9: e48885
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6971: Snowflake yeast 3
6971: Snowflake yeast 3
Multicellular yeast called snowflake yeast that researchers created through many generations of directed evolution from unicellular yeast. Here, the researchers visualized nuclei in orange to help them study changes in how the yeast cells divided. Cell walls are shown in blue. This image was captured using spinning disk confocal microscopy.
Related to images 6969 and 6970.
Related to images 6969 and 6970.
William Ratcliff, Georgia Institute of Technology.
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3606: Flower-forming cells in a small plant related to cabbage (Arabidopsis)
3606: Flower-forming cells in a small plant related to cabbage (Arabidopsis)
In plants, as in animals, stem cells can transform into a variety of different cell types. The stem cells at the growing tip of this Arabidopsis plant will soon become flowers. Arabidopsis is frequently studied by cellular and molecular biologists because it grows rapidly (its entire life cycle is only 6 weeks), produces lots of seeds, and has a genome that is easy to manipulate.
This image was part of the Life: Magnified exhibit that ran from June 3, 2014, to January 21, 2015, at Dulles International Airport.
This image was part of the Life: Magnified exhibit that ran from June 3, 2014, to January 21, 2015, at Dulles International Airport.
Arun Sampathkumar and Elliot Meyerowitz, California Institute of Technology
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2399: Bence Jones protein MLE
2399: Bence Jones protein MLE
A crystal of Bence Jones protein created for X-ray crystallography, which can reveal detailed, three-dimensional protein structures.
Alex McPherson, University of California, Irvine
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2336: Natural nanomachine in action
2336: Natural nanomachine in action
Using a supercomputer to simulate the movement of atoms in a ribosome, researchers looked into the core of this protein-making nanomachine and took snapshots. The picture shows an amino acid (green) being delivered by transfer RNA (yellow) into a corridor (purple) in the ribosome. In the corridor, a series of chemical reactions will string together amino acids to make a protein. The research project, which tracked the movement of more than 2.6 million atoms, was the largest computer simulation of a biological structure to date. The results shed light on the manufacturing of proteins and could aid the search for new antibiotics, which typically work by disabling the ribosomes of bacteria.
Kevin Sanbonmatsu, Los Alamos National Laboratory
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3633: Cells lining the blood vessel walls
3633: Cells lining the blood vessel walls
The structure of the endothelium, the thin layer of cells that line our arteries and veins, is visible here. The endothelium is like a gatekeeper, controlling the movement of materials into and out of the bloodstream. Endothelial cells are held tightly together by specialized proteins that function like strong ropes (red) and others that act like cement (blue).
This image was part of the Life: Magnified exhibit that ran from June 3, 2014, to January 21, 2015, at Dulles International Airport.
This image was part of the Life: Magnified exhibit that ran from June 3, 2014, to January 21, 2015, at Dulles International Airport.
Christopher V. Carman and Roberta Martinelli, Harvard Medical School.
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2702: Thermotoga maritima and its metabolic network
2702: Thermotoga maritima and its metabolic network
A combination of protein structures determined experimentally and computationally shows us the complete metabolic network of a heat-loving bacterium.
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1271: Cone cell
1271: Cone cell
The cone cell of the eye allows you to see in color. Appears in the NIGMS booklet Inside the Cell.
Judith Stoffer
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3307: DNA replication origin recognition complex (ORC)
3307: DNA replication origin recognition complex (ORC)
A study published in March 2012 used cryo-electron microscopy to determine the structure of the DNA replication origin recognition complex (ORC), a semi-circular, protein complex (yellow) that recognizes and binds DNA to start the replication process. The ORC appears to wrap around and bend approximately 70 base pairs of double stranded DNA (red and blue). Also shown is the protein Cdc6 (green), which is also involved in the initiation of DNA replication. The video shows the structure from different angles. See related image 3597.
Huilin Li, Brookhaven National Laboratory
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3567: RSV-Infected Cell
3567: RSV-Infected Cell
Viral RNA (red) in an RSV-infected cell. More information about the research behind this image can be found in a Biomedical Beat Blog posting from January 2014.
Eric Alonas and Philip Santangelo, Georgia Institute of Technology and Emory University
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3603: Salivary gland in the developing fruit fly
3603: Salivary gland in the developing fruit fly
For fruit flies, the salivary gland is used to secrete materials for making the pupal case, the protective enclosure in which a larva transforms into an adult fly. For scientists, this gland provided one of the earliest glimpses into the genetic differences between individuals within a species. Chromosomes in the cells of these salivary glands replicate thousands of times without dividing, becoming so huge that scientists can easily view them under a microscope and see differences in genetic content between individuals.
This image was part of the Life: Magnified exhibit that ran from June 3, 2014, to January 21, 2015, at Dulles International Airport.
This image was part of the Life: Magnified exhibit that ran from June 3, 2014, to January 21, 2015, at Dulles International Airport.
Richard Fehon, University of Chicago
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2339: Protein from Arabidopsis thaliana
2339: Protein from Arabidopsis thaliana
NMR solution structure of a plant protein that may function in host defense. This protein was expressed in a convenient and efficient wheat germ cell-free system. Featured as the June 2007 Protein Structure Initiative Structure of the Month.
Center for Eukaryotic Structural Genomics
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5777: Microsporidia in roundworm 1
5777: Microsporidia in roundworm 1
Many disease-causing microbes manipulate their host’s metabolism and cells for their own ends. Microsporidia—which are parasites closely related to fungi—infect and multiply inside animal cells, and take the rearranging of cells’ interiors to a new level. They reprogram animal cells such that the cells start to fuse, causing them to form long, continuous tubes. As shown in this image of the roundworm Caenorhabditis elegans, microsporidia (shown in magenta) have invaded the worm’s gut cells (shown in yellow; the cells’ nuclei are shown in blue) and have instructed the cells to merge. The cell fusion enables the microsporidia to thrive and propagate in the expanded space. Scientists study microsporidia in worms to gain more insight into how these parasites manipulate their host cells. This knowledge might help researchers devise strategies to prevent or treat infections with microsporidia. For more on the research into microsporidia, see this news release from the University of California San Diego. Related to images 5778 and 5779.
Keir Balla and Emily Troemel, University of California San Diego
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2740: Early life of a protein
2740: Early life of a protein
This illustration represents the early life of a protein—specifically, apomyoglobin—as it is synthesized by a ribosome and emerges from the ribosomal tunnel, which contains the newly formed protein's conformation. The synthesis occurs in the complex swirl of the cell medium, filled with interactions among many molecules. Researchers in Silvia Cavagnero's laboratory are studying the structure and dynamics of newly made proteins and polypeptides using spectroscopic and biochemical techniques.
Silvia Cavagnero, University of Wisconsin, Madison
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