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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.

3585: Relapsing fever bacterium (gray) and red blood cells
3585: Relapsing fever bacterium (gray) and red blood cells
Relapsing fever is caused by a bacterium and transmitted by certain soft-bodied ticks or body lice. The disease is seldom fatal in humans, but it can be very serious and prolonged. This scanning electron micrograph shows Borrelia hermsii (green), one of the bacterial species that causes the disease, interacting with red blood cells. Micrograph by Robert Fischer, NIAID. Related to image 3586.
For more information about relapsing fever, see https://www.cdc.gov/relapsing-fever/index.html.
This image is part of the Life: Magnified collection, which was displayed in the Gateway Gallery at Washington Dulles International Airport June 3, 2014, to January 21, 2015.
For more information about relapsing fever, see https://www.cdc.gov/relapsing-fever/index.html.
This image is part of the Life: Magnified collection, which was displayed in the Gateway Gallery at Washington Dulles International Airport June 3, 2014, to January 21, 2015.
NIAID
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3791: Nucleolus subcompartments spontaneously self-assemble 2
3791: Nucleolus subcompartments spontaneously self-assemble 2
The nucleolus is a small but very important protein complex located in the cell's nucleus. It forms on the chromosomes at the location where the genes for the RNAs are that make up the structure of the ribosome, the indispensable cellular machine that makes proteins from messenger RNAs.
However, how the nucleolus grows and maintains its structure has puzzled scientists for some time. It turns out that even though it looks like a simple liquid blob, it's rather well-organized, consisting of three distinct layers: the fibrillar center, where the RNA polymerase is active; the dense fibrillar component, which is enriched in the protein fibrillarin; and the granular component, which contains a protein called nucleophosmin. Researchers have now discovered that this multilayer structure of the nucleolus arises from differences in how the proteins in each compartment mix with water and with each other. These differences let the proteins readily separate from each other into the three nucleolus compartments.
This video of nucleoli in the eggs of a commonly used lab animal, the frog Xenopus laevis, shows how each of the compartments (the granular component is shown in red, the fibrillarin in yellow-green, and the fibrillar center in blue) spontaneously fuse with each other on encounter without mixing with the other compartments.
For more details on this research, see this press release from Princeton. Related to video 3789, image 3792 and image 3793.
However, how the nucleolus grows and maintains its structure has puzzled scientists for some time. It turns out that even though it looks like a simple liquid blob, it's rather well-organized, consisting of three distinct layers: the fibrillar center, where the RNA polymerase is active; the dense fibrillar component, which is enriched in the protein fibrillarin; and the granular component, which contains a protein called nucleophosmin. Researchers have now discovered that this multilayer structure of the nucleolus arises from differences in how the proteins in each compartment mix with water and with each other. These differences let the proteins readily separate from each other into the three nucleolus compartments.
This video of nucleoli in the eggs of a commonly used lab animal, the frog Xenopus laevis, shows how each of the compartments (the granular component is shown in red, the fibrillarin in yellow-green, and the fibrillar center in blue) spontaneously fuse with each other on encounter without mixing with the other compartments.
For more details on this research, see this press release from Princeton. Related to video 3789, image 3792 and image 3793.
Nilesh Vaidya, Princeton University
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3615: An insect tracheal cell delivers air to muscles
3615: An insect tracheal cell delivers air to muscles
Insects like the fruit fly use an elaborate network of branching tubes called trachea (green) to transport oxygen throughout their bodies. Fruit flies have been used in biomedical research for more than 100 years and remain one of the most frequently studied model organisms. They have a large percentage of genes in common with us, including hundreds of genes that are associated with human diseases.
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.
Jayan Nair and Maria Leptin, European Molecular Biology Laboratory, Heidelberg, Germany
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3290: Three neurons and human ES cells
3290: Three neurons and human ES cells
The three neurons (red) visible in this image were derived from human embryonic stem cells. Undifferentiated stem cells are green here. Image and caption information courtesy of the California Institute for Regenerative Medicine.
Anirvan Ghosh lab, University of California, San Diego, via CIRM
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1291: Olfactory system
1291: Olfactory system
Sensory organs have cells equipped for detecting signals from the environment, such as odors. Receptors in the membranes of nerve cells in the nose bind to odor molecules, triggering a cascade of chemical reactions tranferred by G proteins into the cytoplasm.
Judith Stoffer
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2739: Tetrapolar mitosis
2739: Tetrapolar mitosis
This image shows an abnormal, tetrapolar mitosis. Chromosomes are highlighted pink. The cells shown are S3 tissue cultured cells from Xenopus laevis, African clawed frog.
Gary Gorbsky, Oklahoma Medical Research Foundation
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2558: RNA interference
2558: RNA interference
RNA interference or RNAi is a gene-silencing process in which double-stranded RNAs trigger the destruction of specific RNAs. See 2559 for a labeled version of this illustration. Featured in The New Genetics.
Crabtree + Company
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5800: Mouse cerebellum in pink and blue
5800: Mouse cerebellum in pink and blue
The cerebellum is the brain's locomotion control center. Found at the base of your brain, the cerebellum is a single layer of tissue with deep folds like an accordion. People with damage to this region of the brain often have difficulty with balance, coordination and fine motor skills.
This image of a mouse cerebellum is part of a collection of such images in different colors and at different levels of magnification from the National Center for Microscopy and Imaging Research (NCMIR). Related to image 5795.
This image of a mouse cerebellum is part of a collection of such images in different colors and at different levels of magnification from the National Center for Microscopy and Imaging Research (NCMIR). Related to image 5795.
National Center for Microscopy and Imaging Research (NCMIR)
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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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3363: Dopamine D3 receptor
3363: Dopamine D3 receptor
The receptor is shown bound to an antagonist, eticlopride
Raymond Stevens, The Scripps Research Institute
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1314: Chromosomes after crossing over
1314: Chromosomes after crossing over
Duplicated pair of chromosomes have exchanged material.
Judith Stoffer
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3592: Math from the heart
3592: Math from the heart
Watch a cell ripple toward a beam of light that turns on a movement-related protein.
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6593: Cell-like compartments from frog eggs 6
6593: Cell-like compartments from frog eggs 6
Cell-like compartments that spontaneously emerged from scrambled frog eggs, with nuclei (blue) from frog sperm. Endoplasmic reticulum (red) and microtubules (green) are also visible. Image created using confocal microscopy.
For more photos of cell-like compartments from frog eggs view: 6584, 6585, 6586, 6591, 6592.
For videos of cell-like compartments from frog eggs view: 6587, 6588, 6589, and 6590.
Xianrui Cheng, Stanford University School of Medicine.
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3399: Synapses in culture
3399: Synapses in culture
Cultured hippocampal neurons grown on a substrate of glial cells (astrocytes). The glial cells form the pink/brown underlayment in this image. The tan threads are the neurons. The round tan balls are synapses, the points where neurons meet and communicate with each other. The cover slip underlying the cells is green. Neurons in culture can be used to study synaptic plasticity, activity-dependent protein turnover, and other topics in neuroscience.
National Center for Microscopy and Imaging Research
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1120: Superconducting magnet
1120: Superconducting magnet
Superconducting magnet for NMR research, from the February 2003 profile of Dorothee Kern in Findings.
Mike Lovett
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3792: Nucleolus subcompartments spontaneously self-assemble 3
3792: Nucleolus subcompartments spontaneously self-assemble 3
What looks a little like distant planets with some mysterious surface features are actually assemblies of proteins normally found in the cell's nucleolus, a small but very important protein complex located in the cell's nucleus. It forms on the chromosomes at the location where the genes for the RNAs are that make up the structure of the ribosome, the indispensable cellular machine that makes proteins from messenger RNAs.
However, how the nucleolus grows and maintains its structure has puzzled scientists for some time. It turns out that even though it looks like a simple liquid blob, it's rather well-organized, consisting of three distinct layers: the fibrillar center, where the RNA polymerase is active; the dense fibrillar component, which is enriched in the protein fibrillarin; and the granular component, which contains a protein called nucleophosmin. Researchers have now discovered that this multilayer structure of the nucleolus arises from differences in how the proteins in each compartment mix with water and with each other. These differences let the proteins readily separate from each other into the three nucleolus compartments.
This photo of nucleolus proteins in the eggs of a commonly used lab animal, the frog Xenopus laevis, shows each of the nucleolus compartments (the granular component is shown in red, the fibrillarin in yellow-green, and the fibrillar center in blue). The researchers have found that these compartments spontaneously fuse with each other on encounter without mixing with the other compartments.
For more details on this research, see this press release from Princeton. Related to video 3789, video 3791 and image 3793.
However, how the nucleolus grows and maintains its structure has puzzled scientists for some time. It turns out that even though it looks like a simple liquid blob, it's rather well-organized, consisting of three distinct layers: the fibrillar center, where the RNA polymerase is active; the dense fibrillar component, which is enriched in the protein fibrillarin; and the granular component, which contains a protein called nucleophosmin. Researchers have now discovered that this multilayer structure of the nucleolus arises from differences in how the proteins in each compartment mix with water and with each other. These differences let the proteins readily separate from each other into the three nucleolus compartments.
This photo of nucleolus proteins in the eggs of a commonly used lab animal, the frog Xenopus laevis, shows each of the nucleolus compartments (the granular component is shown in red, the fibrillarin in yellow-green, and the fibrillar center in blue). The researchers have found that these compartments spontaneously fuse with each other on encounter without mixing with the other compartments.
For more details on this research, see this press release from Princeton. Related to video 3789, video 3791 and image 3793.
Nilesh Vaidya, Princeton University
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6521: Yeast art depicting the New York City skyline
6521: Yeast art depicting the New York City skyline
This skyline of New York City was created by “printing” nanodroplets containing yeast (Saccharomyces cerevisiae) onto a large plate. Each dot is a separate yeast colony. As the colonies grew, a picture emerged, creating art. To make the different colors shown here, yeast strains were genetically engineered to produce pigments naturally made by bacteria, fungi, and sea creatures such as coral and sea anemones. Using genes from other organisms to make biological compounds paves the way toward harnessing yeast in the production of other useful molecules, from food to fuels and drugs.
Michael Shen, Ph.D., Jasmine Temple, Leslie Mitchell, Ph.D., and Jef Boeke, Ph.D., New York University School of Medicine; and Nick Phillips, James Chuang, Ph.D., and Jiarui Wang, Johns Hopkins University.
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3664: Mitochondria from rat heart muscle cell_2
3664: Mitochondria from rat heart muscle cell_2
These mitochondria (brown) are from the heart muscle cell of a rat. Mitochondria have an inner membrane that folds in many places (and that appears here as striations). This folding vastly increases the surface area for energy production. Nearly all our cells have mitochondria. Related to image 3661.
National Center for Microscopy and Imaging Research
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6571: Actin filaments bundled around the dynamin helical polymer
6571: Actin filaments bundled around the dynamin helical polymer
Multiple actin filaments (magenta) are organized around a dynamin helical polymer (rainbow colored) in this model derived from cryo-electron tomography. By bundling actin, dynamin increases the strength of a cell’s skeleton and plays a role in cell-cell fusion, a process involved in conception, development, and regeneration.
Elizabeth Chen, University of Texas Southwestern Medical Center.
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6555: Floral pattern in a mixture of two bacterial species, Acinetobacter baylyi and Escherichia coli, grown on a semi-solid agar for 48 hours (photo 2)
6555: Floral pattern in a mixture of two bacterial species, Acinetobacter baylyi and Escherichia coli, grown on a semi-solid agar for 48 hours (photo 2)
Floral pattern emerging as two bacterial species, motile Acinetobacter baylyi (red) and non-motile Escherichia coli (green), are grown together for 48 hours on 1% 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 another photo of this process at 48 hours on 1% agar surface.
See 6556 for a photo of this process at 72 hours on 0.5% 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 another photo of this process at 48 hours on 1% agar surface.
See 6556 for a photo of this process at 72 hours on 0.5% agar surface.
See 6550 for a video of this process.
L. Xiong et al, eLife 2020;9: e48885
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2453: Seeing signaling protein activation in cells 03
2453: Seeing signaling protein activation in cells 03
Cdc42, a member of the Rho family of small guanosine triphosphatase (GTPase) proteins, regulates multiple cell functions, including motility, proliferation, apoptosis, and cell morphology. In order to fulfill these diverse roles, the timing and location of Cdc42 activation must be tightly controlled. Klaus Hahn and his research group use special dyes designed to report protein conformational changes and interactions, here in living neutrophil cells. Warmer colors in this image indicate higher levels of activation. Cdc42 looks to be activated at cell protrusions.
Related to images 2451, 2452, and 2454.
Related to images 2451, 2452, and 2454.
Klaus Hahn, University of North Carolina, Chapel Hill Medical School
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2551: Introns (with labels)
2551: Introns (with labels)
Genes are often interrupted by stretches of DNA (introns, blue) that do not contain instructions for making a protein. The DNA segments that do contain protein-making instructions are known as exons (green). See image 2550 for an unlabeled version of this illustration. Featured in The New Genetics.
Crabtree + Company
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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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5753: Clathrin-mediated endocytosis
5753: Clathrin-mediated endocytosis
Endocytosis is the process by which cells are able to take up membrane and extracellular materials through the formation of a small intracellular bubble, called a vesicle. This process, called membrane budding, is generally by a coating of proteins. This protein coat helps both to deform the membrane and to concentrate specific proteins inside the newly forming vesicle. Clathrin is a coat protein that functions in receptor-mediated endocytosis events at the plasma membrane. This animation shows the process of clathrin-mediated endocytosis. An iron-transport protein called transferrin (blue) is bound to its receptor (purple) on the exterior cell membrane. Inside the cell, a clathrin cage (shown in white/beige) assembles through interactions with membrane-bound adaptor proteins (green), causing the cell membrane to begin bending. The adaptor proteins also bind to receptors for transferrin, capturing them in the growing vesicle. Molecules of a protein called dynamin (purple) are then recruited to the neck of the vesicle and are involved in separating the membranes of the cell and the vesicle. Soon after the vesicle has budded off the membrane, the clathrin cage is disassembled. This disassembly is mediated by another protein called HSC70 (yellow), and its cofactor protein auxilin (orange).
Janet Iwasa, University of Utah
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3437: Network diagram of genes, cellular components and processes (labeled)
3437: Network diagram of genes, cellular components and processes (labeled)
This image shows the hierarchical ontology of genes, cellular components and processes derived from large genomic datasets. From Dutkowski et al. A gene ontology inferred from molecular networks Nat Biotechnol. 2013 Jan;31(1):38-45. Related to 3436.
Janusz Dutkowski and Trey Ideker, University of California, San Diego
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2509: From DNA to Protein
2509: From DNA to Protein
Nucleotides in DNA are copied into RNA, where they are read three at a time to encode the amino acids in a protein. Many parts of a protein fold as the amino acids are strung together.
See image 2510 for a labeled version of this illustration.
Featured in The Structures of Life.
See image 2510 for a labeled version of this illustration.
Featured in The Structures of Life.
Crabtree + Company
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3498: Wound healing in process
3498: Wound healing in process
Wound healing requires the action of stem cells. In mice that lack the Sept2/ARTS gene, stem cells involved in wound healing live longer and wounds heal faster and more thoroughly than in normal mice. This confocal microscopy image from a mouse lacking the Sept2/ARTS gene shows a tail wound in the process of healing. See more information in the article in Science.
Related to images 3497 and 3500.
Related to images 3497 and 3500.
Hermann Steller, Rockefeller University
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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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2396: Hen egg lysozyme (1)
2396: Hen egg lysozyme (1)
Crystals of hen egg lysozyme protein created for X-ray crystallography, which can reveal detailed, three-dimensional protein structures.
Alex McPherson, University of California, Irvine
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3500: Wound healing in process
3500: Wound healing in process
Wound healing requires the action of stem cells. In mice that lack the Sept2/ARTS gene, stem cells involved in wound healing live longer and wounds heal faster and more thoroughly than in normal mice. This confocal microscopy image from a mouse lacking the Sept2/ARTS gene shows a tail wound in the process of healing. See more information in the article in Science.
Related to images 3497 and 3498.
Related to images 3497 and 3498.
Hermann Steller, Rockefeller University
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2313: Colorful communication
2313: Colorful communication
The marine bacterium Vibrio harveyi glows when near its kind. This luminescence, which results from biochemical reactions, is part of the chemical communication used by the organisms to assess their own population size and distinguish themselves from other types of bacteria. But V. harveyi only light up when part of a large group. This communication, called quorum sensing, speaks for itself here on a lab dish, where more densely packed areas of the bacteria show up blue. Other types of bacteria use quorum sensing to release toxins, trigger disease, and evade the immune system.
Bonnie Bassler, Princeton University
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5772: Confocal microscopy image of two Drosophila ovarioles
5772: Confocal microscopy image of two Drosophila ovarioles
Ovarioles in female insects are tubes in which egg cells (called oocytes) form at one end and complete their development as they reach the other end of the tube. This image, taken with a confocal microscope, shows ovarioles in a very popular lab animal, the fruit fly Drosophila. The basic structure of ovarioles supports very rapid egg production, with some insects (like termites) producing several thousand eggs per day. Each insect ovary typically contains four to eight ovarioles, but this number varies widely depending on the insect species.
Scientists use insect ovarioles, for example, to study the basic processes that help various insects, including those that cause disease (like some mosquitos and biting flies), reproduce very quickly.
Scientists use insect ovarioles, for example, to study the basic processes that help various insects, including those that cause disease (like some mosquitos and biting flies), reproduce very quickly.
2004 Olympus BioScapes Competition
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3283: Mouse heart muscle cells 02
3283: Mouse heart muscle cells 02
This image shows neonatal mouse heart cells. These cells were grown in the lab on a chip that aligns the cells in a way that mimics what is normally seen in the body. Green shows the muscle protein toponin I. Red indicates the muscle protein actin, and blue indicates the cell nuclei. The work shown here was part of a study attempting to grow heart tissue in the lab to repair damage after a heart attack. Image and caption information courtesy of the California Institute for Regenerative Medicine. Related to images 3281 and 3282.
Kara McCloskey lab, University of California, Merced, via CIRM
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1329: Mitosis - metaphase
1329: Mitosis - metaphase
A cell in metaphase during mitosis: The copied chromosomes align in the middle of the spindle. Mitosis is responsible for growth and development, as well as for replacing injured or worn out cells throughout the body. For simplicity, mitosis is illustrated here with only six chromosomes.
Judith Stoffer
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2374: Protein from Methanobacterium thermoautotrophicam
2374: Protein from Methanobacterium thermoautotrophicam
A knotted protein from an archaebacterium called Methanobacterium thermoautotrophicam. This organism breaks down waste products and produces methane gas. Protein folding theory previously held that forming a knot was beyond the ability of a protein, but this structure, determined at Argonne's Structural Biology Center, proves differently. Researchers theorize that this knot stabilizes the amino acid subunits of the protein.
Midwest Center For Structural Genomics, PSI
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2521: Enzymes convert subtrates into products
2521: Enzymes convert subtrates into products
Enzymes convert substrates into products very quickly. See image 2522 for a labeled version of this illustration. Featured in The Chemistry of Health.
Crabtree + Company
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2523: Plasma membrane
2523: Plasma membrane
The plasma membrane is a cell's protective barrier. See image 2524 for a labeled version of this illustration. Featured in The Chemistry of Health.
Crabtree + Company
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6770: Group of Culex quinquefasciatus mosquito larvae
6770: Group of Culex quinquefasciatus mosquito larvae
Mosquito larvae with genes edited by CRISPR. This species of mosquito, Culex quinquefasciatus, can transmit West Nile virus, Japanese encephalitis virus, and avian malaria, among other diseases. The researchers who took this image developed a gene-editing toolkit for Culex quinquefasciatus that could ultimately help stop the mosquitoes from spreading pathogens. The work is described in the Nature Communications paper "Optimized CRISPR tools and site-directed transgenesis towards gene drive development in Culex quinquefasciatus mosquitoes" by Feng et al. Related to image 6769 and video 6771.
Valentino Gantz, University of California, San Diego.
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1015: Lily mitosis 05
1015: Lily mitosis 05
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. Here, condensed chromosomes are clearly visible.
Related to images 1010, 1011, 1012, 1013, 1014, 1016, 1017, 1018, 1019, and 1021.
Related to images 1010, 1011, 1012, 1013, 1014, 1016, 1017, 1018, 1019, and 1021.
Andrew S. Bajer, University of Oregon, Eugene
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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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3621: Q fever bacteria in an infected cell
3621: Q fever bacteria in an infected cell
This image shows Q fever bacteria (yellow), which infect cows, sheep, and goats around the world and can infect humans, as well. When caught early, Q fever can be cured with antibiotics. A small fraction of people can develop a more serious, chronic form of the disease.
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.
Robert Heinzen, Elizabeth Fischer, and Anita Mora, National Institute of Allergy and Infectious Diseases, National Institutes of Health
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5875: Bacteriophage P22 capsid, detail
5875: Bacteriophage P22 capsid, detail
Detail of a subunit of the capsid, or outer cover, of bacteriophage P22, a virus that infects the Salmonella bacteria. Cryo-electron microscopy (cryo-EM) was used to capture details of the capsid proteins, each shown here in a separate color. Thousands of cryo-EM scans capture the structure and shape of all the individual proteins in the capsid and their position relative to other proteins. A computer model combines these scans into the image shown here. Related to image 5874.
Dr. Wah Chiu, Baylor College of Medicine
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6804: Staphylococcus aureus in the porous coating of a femoral hip stem
6804: Staphylococcus aureus in the porous coating of a femoral hip stem
Staphylococcus aureus bacteria (blue) on the porous coating of a femoral hip stem used in hip replacement surgery. The relatively rough surface of an implant is a favorable environment for bacteria to attach and grow. This can lead to the development of biofilms, which can cause infections. The researchers who took this image are working to understand where biofilms are likely to develop. This knowledge could support the prevention and treatment of infections. A scanning electron microscope was used to capture this image.
More information on the research that produced this image can be found in the Antibiotics paper "Free-floating aggregate and single-cell-initiated biofilms of Staphylococcus aureus" by Gupta et al.
Related to image 6803 and video 6805.
More information on the research that produced this image can be found in the Antibiotics paper "Free-floating aggregate and single-cell-initiated biofilms of Staphylococcus aureus" by Gupta et al.
Related to image 6803 and video 6805.
Paul Stoodley, The Ohio State University.
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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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2515: Life of an AIDS virus (with labels and stages)
2515: Life of an AIDS virus (with labels and stages)
HIV is a retrovirus, a type of virus that carries its genetic material not as DNA but as RNA. Long before anyone had heard of HIV, researchers in labs all over the world studied retroviruses, tracing out their life cycle and identifying the key proteins the viruses use to infect cells. When HIV was identified as a retrovirus, these studies gave AIDS researchers an immediate jump-start. The previously identified viral proteins became initial drug targets. See images 2513 and 2514 for other versions of this illustration. Featured in The Structures of Life.
Crabtree + Company
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3764: Movie of the 19S proteasome subunit processing a protein substrate
3764: Movie of the 19S proteasome subunit processing a protein substrate
The proteasome is a critical multiprotein complex in the cell that breaks down and recycles proteins that have become damaged or are no longer needed. This movie shows how a protein substrate (red) is bound through its ubiquitin chain (blue) to one of the ubiquitin receptors of the proteasome (Rpn10, yellow). The substrate's flexible engagement region then gets engaged by the AAA+ motor of the proteasome (cyan), which initiates mechanical pulling, unfolding and movement of the protein into the proteasome's interior for cleavage into shorter protein pieces called peptides. During movement of the substrate, its ubiquitin modification gets cleaved off by the deubiquitinase Rpn11 (green), which sits directly above the entrance to the AAA+ motor pore and acts as a gatekeeper to ensure efficient ubiquitin removal, a prerequisite for fast protein breakdown by the 26S proteasome. Related to image 3763.
Andreas Martin, HHMI
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3779: Precisely Delivering Chemical Cargo to Cells
3779: Precisely Delivering Chemical Cargo to Cells
Moving protein or other molecules to specific cells to treat or examine them has been a major biological challenge. Scientists have now developed a technique for delivering chemicals to individual cells. The approach involves gold nanowires that, for example, can carry tumor-killing proteins. The advance was possible after researchers developed electric tweezers that could manipulate gold nanowires to help deliver drugs to single cells.
This movie shows the manipulation of the nanowires for drug delivery to a single cell. To learn more about this technique, see this post in the Computing Life series.
This movie shows the manipulation of the nanowires for drug delivery to a single cell. To learn more about this technique, see this post in the Computing Life series.
Nature Nanotechnology
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6933: Zebrafish head vasculature video
6933: Zebrafish head vasculature video
Various views of 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 video was captured using a light sheet microscope.
Related to image 6934.
This video was captured using a light sheet microscope.
Related to image 6934.
Prayag Murawala, MDI Biological Laboratory and Hannover Medical School.
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1290: Nucleus and rough ER
1290: Nucleus and rough ER
The nucleus contains the DNA of eukaryotic cells. The double membrane that bounds the nucleus flows into the rough endoplasmic reticulum, an organelle studded with ribosomes that manufacture membrane-bound proteins for the rest of the cell.
Judith Stoffer
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