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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.
6550: Time-lapse video of floral pattern in a mixture of two bacterial species, Acinetobacter baylyi and Escherichia coli, grown on a semi-solid agar for 24 hours
6550: Time-lapse video of floral pattern in a mixture of two bacterial species, Acinetobacter baylyi and Escherichia coli, grown on a semi-solid agar for 24 hours
This time-lapse video shows the emergence of a flower-like pattern in a mixture of two bacterial species, motile Acinetobacter baylyi and non-motile Escherichia coli (green), that are grown together for 24 hours on 0.75% 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 6556 for a photo of this process at 72 hours on 0.5% agar surface.
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 6556 for a photo of this process at 72 hours on 0.5% agar surface.
L. Xiong et al, eLife 2020;9: e48885
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7022: Single-cell “radios” video
7022: Single-cell “radios” video
Individual cells are color-coded based on their identity and signaling activity using a protein circuit technology developed by the Coyle Lab. Just as a radio allows you to listen to an individual frequency, this technology allows researchers to tune into the specific “radio station” of each cell through genetically encoded proteins from a bacterial system called MinDE. The proteins generate an oscillating fluorescent signal that transmits information about cell shape, state, and identity that can be decoded using digital signal processing tools originally designed for telecommunications. The approach allows researchers to look at the dynamics of a single cell in the presence of many other cells.
Related to image 7021.
Related to image 7021.
Scott Coyle, University of Wisconsin-Madison.
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3360: H1 histamine receptor
3360: H1 histamine receptor
The receptor is shown bound to an inverse agonist, doxepin.
Raymond Stevens, The Scripps Research Institute
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1334: Aging book of life
1334: Aging book of life
Damage to each person's genome, often called the "Book of Life," accumulates with time. Such DNA mutations arise from errors in the DNA copying process, as well as from external sources, such as sunlight and cigarette smoke. DNA mutations are known to cause cancer and also may contribute to cellular aging.
Judith Stoffer
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5795: Mouse cerebellum
5795: Mouse cerebellum
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 5800.
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 5800.
National Center for Microscopy and Imaging Research (NCMIR)
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3644: Zebrafish embryo
3644: Zebrafish embryo
Just 22 hours after fertilization, this zebrafish embryo is already taking shape. By 36 hours, all of the major organs will have started to form. The zebrafish's rapid growth and see-through embryo make it ideal for scientists studying how organs develop.
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.
Philipp Keller, Bill Lemon, Yinan Wan, and Kristin Branson, Janelia Farm Research Campus, Howard Hughes Medical Institute, Ashburn, Va.
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6602: See how immune cell acid destroys bacterial proteins
6602: See how immune cell acid destroys bacterial proteins
This animation shows the effect of exposure to hypochlorous acid, which is found in certain types of immune cells, on bacterial proteins. The proteins unfold and stick to one another, leading to cell death.
American Chemistry Council
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2802: Biosensors illustration
2802: Biosensors illustration
A rendering of an activity biosensor image overlaid with a cell-centered frame of reference used for image analysis of signal transduction. This is an example of NIH-supported research on single-cell analysis. Related to 2798 , 2799, 2800, 2801 and 2803.
Gaudenz Danuser, Harvard Medical School
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5780: Ribosome illustration from PDB
5780: Ribosome illustration from PDB
Ribosomes are complex machines made up of more than 50 proteins and three or four strands of genetic material called ribosomal RNA (rRNA). The busy cellular machines make proteins, which are critical to almost every structure and function in the cell. To do so, they read protein-building instructions, which come as strands of messenger RNA. Ribosomes are found in all forms of cellular life—people, plants, animals, even bacteria. This illustration of a bacterial ribosome was produced using detailed information about the position of every atom in the complex. Several antibiotic medicines work by disrupting bacterial ribosomes but leaving human ribosomes alone. Scientists are carefully comparing human and bacterial ribosomes to spot differences between the two. Structures that are present only in the bacterial version could serve as targets for new antibiotic medications.
From PDB’s Molecule of the Month collection (direct link: http://pdb101.rcsb.org/motm/121) Molecule of the Month illustrations are available under a CC-BY-4.0 license. Attribution should be given to David S. Goodsell and the RCSB PDB.
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2307: Cells frozen in time
2307: Cells frozen in time
The fledgling field of X-ray microscopy lets researchers look inside whole cells rapidly frozen to capture their actions at that very moment. Here, a yeast cell buds before dividing into two. Colors show different parts of the cell. Seeing whole cells frozen in time will help scientists observe cells' complex structures and follow how molecules move inside them.
Carolyn Larabell, University of California, San Francisco, and the Lawrence Berkeley National Laboratory
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3738: Transmission electron microscopy of coronary artery wall with elastin-rich ECM pseudocolored in light brown
3738: Transmission electron microscopy of coronary artery wall with elastin-rich ECM pseudocolored in light brown
Elastin is a fibrous protein in the extracellular matrix (ECM). It is abundant in artery walls like the one shown here. As its name indicates, elastin confers elasticity. Elastin fibers are at least five times stretchier than rubber bands of the same size. Tissues that expand, such as blood vessels and lungs, need to be both strong and elastic, so they contain both collagen (another ECM protein) and elastin. In this photo, the elastin-rich ECM is colored grayish brown and is most visible at the bottom of the photo. The curved red structures near the top of the image are red blood cells.
Tom Deerinck, National Center for Microscopy and Imaging Research (NCMIR)
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2386: Sortase b from B. anthracis
2386: Sortase b from B. anthracis
Structure of sortase b from the bacterium B. anthracis, which causes anthrax. Sortase b is an enzyme used to rob red blood cells of iron, which the bacteria need to survive.
Midwest Center for Structural Genomics, PSI
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6613: Circadian rhythms and the SCN
6613: Circadian rhythms and the SCN
Circadian rhythms are physical, mental, and behavioral changes that follow a 24-hour cycle. Circadian rhythms are influenced by light and regulated by the brain’s suprachiasmatic nucleus (SCN), sometimes referred to as a master clock. Learn more in NIGMS’ circadian rhythms fact sheet. See 6614 for the Spanish version of this infographic.
NIGMS
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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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3634: Cells use bubble-like structures called vesicles to transport cargo
3634: Cells use bubble-like structures called vesicles to transport cargo
Cells use bubble-like structures called vesicles (yellow) to import, transport, and export cargo and in cellular communication. A single cell may be filled with thousands of moving vesicles.
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.
Tatyana Svitkina, University of Pennsylvania
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6807: Fruit fly ovaries
6807: Fruit fly ovaries
Fruit fly (Drosophila melanogaster) ovaries with DNA shown in magenta and actin filaments shown in light blue. This image was captured using a confocal laser scanning microscope.
Related to image 6806.
Related to image 6806.
Vladimir I. Gelfand, Feinberg School of Medicine, Northwestern 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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6572: Nuclear Lamina
6572: Nuclear Lamina
The 3D single-molecule super-resolution reconstruction of the entire nuclear lamina in a HeLa cell was acquired using the TILT3D platform. TILT3D combines a tilted light sheet with point-spread function (PSF) engineering to provide a flexible imaging platform for 3D single-molecule super-resolution imaging in mammalian cells.
See 6573 for 3 separate views of this structure.
See 6573 for 3 separate views of this structure.
Anna-Karin Gustavsson, Ph.D.
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6791: Yeast cells entering mitosis
6791: Yeast cells entering mitosis
Yeast cells entering mitosis, also known as cell division. The green and magenta dots are two proteins that play important roles in mitosis. They show where the cells will split. This image was captured using wide-field microscopy with deconvolution.
Related to images 6792, 6793, 6794, 6797, 6798, and videos 6795 and 6796.
Related to images 6792, 6793, 6794, 6797, 6798, and videos 6795 and 6796.
Alaina Willet, Kathy Gould’s lab, Vanderbilt University.
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1158: Bacteria shapes
1158: Bacteria shapes
A colorized scanning electron micrograph of bacteria. Scanning electron microscopes allow scientists to see the three-dimensional surface of their samples.
Tina Weatherby Carvalho, University of Hawaii at Manoa
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1284: Ion channels
1284: Ion channels
The body uses a variety of ion channels to transport small molecules across cell membranes.
Judith Stoffer
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3364: Nociceptin/orphanin FQ peptide opioid receptor
3364: Nociceptin/orphanin FQ peptide opioid receptor
The receptor is shown bound to an antagonist, compound-24
Raymond Stevens, The Scripps Research Institute
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6519: Human fibroblast undergoing cell division
6519: Human fibroblast undergoing cell division
During cell division, cells physically divide after separating their genetic material to create two daughter cells that are genetically identical to the parent cell. This process is important so that new cells can grow and develop. In this image, a human fibroblast cell—a type of connective tissue cell that plays a key role in wound healing and tissue repair—is dividing into two daughter cells. A cell protein called actin appears gray, the myosin II (part of the family of motor proteins responsible for muscle contractions) appears green, and DNA appears magenta.
Nilay Taneja, Vanderbilt University, and Dylan T. Burnette, Ph.D., Vanderbilt University School of Medicine.
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3389: NCMIR Intestine-1
3389: NCMIR Intestine-1
The small intestine is where most of our nutrients from the food we eat are absorbed into the bloodstream. The walls of the intestine contain small finger-like projections called villi which increase the organ's surface area, enhancing nutrient absorption. It consists of the duodenum, which connects to the stomach, the jejenum and the ileum, which connects with the large intestine. Related to image 3390.
Tom Deerinck, National Center for Microscopy and Imaging Research (NCMIR)
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5760: Annotated TEM cross-section of C. elegans (roundworm)
5760: Annotated TEM cross-section of C. elegans (roundworm)
The worm Caenorhabditis elegans is a popular laboratory animal because its small size and fairly simple body make it easy to study. Scientists use this small worm to answer many research questions in developmental biology, neurobiology, and genetics. This image, which was taken with transmission electron microscopy (TEM), shows a cross-section through C. elegans, revealing various internal structures labeled in the image. You can find a high-resolution image without the annotations at image 5759.
The image is from a figure in an article published in the journal eLife.
The image is from a figure in an article published in the journal eLife.
Piali Sengupta, Brandeis University
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3793: Nucleolus subcompartments spontaneously self-assemble 4
3793: Nucleolus subcompartments spontaneously self-assemble 4
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 3792.
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 3792.
Nilesh Vaidya, Princeton University
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3297: Four timepoints in gastrulation
3297: Four timepoints in gastrulation
It has been said that gastrulation is the most important event in a person's life. This part of early embryonic development transforms a simple ball of cells and begins to define cell fate and the body axis. In a study published in Science magazine in March 2012, NIGMS grantee Bob Goldstein and his research group studied how contractions of actomyosin filaments in C. elegans and Drosophila embryos lead to dramatic rearrangements of cell and embryonic structure. This research is described in detail in the following article: "Triggering a Cell Shape Change by Exploiting Preexisting Actomyosin Contractions." In these images, myosin (green) and plasma membrane (red) are highlighted at four timepoints in gastrulation in the roundworm C. elegans. The blue highlights in the top three frames show how cells are internalized, and the site of closure around the involuting cells is marked with an arrow in the last frame. See related video 3334.
Bob Goldstein, University of North Carolina, Chapel Hill
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6997: Shiga toxin
6997: Shiga toxin
E. coli bacteria normally live harmlessly in our intestines, but some cause disease by making toxins. One of these toxins, called Shiga toxin (green), inactivates host ribosomes (purple) by mimicking their normal binding partners, the EF-Tu elongation factor (red) complexed with Phe-tRNAPhe (orange).
Find these in the RCSB Protein Data Bank: Shiga toxin 2 (PDB entry 7U6V) and Phe-tRNA (PDB entry 1TTT).
More information about this work can be found in the J. Biol. Chem. paper "Cryo-EM structure of Shiga toxin 2 in complex with the native ribosomal P-stalk reveals residues involved in the binding interaction" by Kulczyk et. al.
Find these in the RCSB Protein Data Bank: Shiga toxin 2 (PDB entry 7U6V) and Phe-tRNA (PDB entry 1TTT).
More information about this work can be found in the J. Biol. Chem. paper "Cryo-EM structure of Shiga toxin 2 in complex with the native ribosomal P-stalk reveals residues involved in the binding interaction" by Kulczyk et. al.
Amy Wu and Christine Zardecki, RCSB Protein Data Bank.
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6750: C. elegans with blue and yellow lights in the background
6750: C. elegans with blue and yellow lights in the background
These microscopic roundworms, called Caenorhabditis elegans, lack eyes and the opsin proteins used by visual systems to detect colors. However, researchers found that the worms can still sense the color of light in a way that enables them to avoid pigmented toxins made by bacteria. This image was captured using a stereo microscope.
H. Robert Horvitz and Dipon Ghosh, Massachusetts Institute of Technology.
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2385: Heat shock protein complex from Methanococcus jannaschii
2385: Heat shock protein complex from Methanococcus jannaschii
Model based on X-ray crystallography of the structure of a small heat shock protein complex from the bacteria, Methanococcus jannaschii. Methanococcus jannaschii is an organism that lives at near boiling temperature, and this protein complex helps it cope with the stress of high temperature. Similar complexes are produced in human cells when they are "stressed" by events such as burns, heart attacks, or strokes. The complexes help cells recover from the stressful event.
Berkeley Structural Genomics Center, PSI-1
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2360: Cell-free protein synthesizers
2360: Cell-free protein synthesizers
Both instruments shown were developed by CellFree Sciences of Yokohama, Japan. The instrument on the left, the GeneDecoder 1000, can generate 384 proteins from their corresponding genes, or gene fragments, overnight. It is used to screen for properties such as level of protein production and degree of solubility. The instrument on the right, the Protemist Protein Synthesizer, is used to generate the larger amounts of protein needed for protein structure determinations.
Center for Eukaryotic Structural Genomics
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6754: Fruit fly nurse cells transporting their contents during egg development
6754: Fruit fly nurse cells transporting their contents during egg development
In many animals, the egg cell develops alongside sister cells. These sister cells are called nurse cells in the fruit fly (Drosophila melanogaster), and their job is to “nurse” an immature egg cell, or oocyte. Toward the end of oocyte development, the nurse cells transfer all their contents into the oocyte in a process called nurse cell dumping. This video captures this transfer, showing significant shape changes on the part of the nurse cells (blue), which are powered by wavelike activity of the protein myosin (red). Researchers created the video using a confocal laser scanning microscope. Related to image 6753.
Adam C. Martin, Massachusetts Institute of Technology.
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2571: VDAC video 02
2571: VDAC video 02
This video shows the structure of the pore-forming protein VDAC-1 from humans. This molecule mediates the flow of products needed for metabolism--in particular the export of ATP--across the outer membrane of mitochondria, the power plants for eukaryotic cells. VDAC-1 is involved in metabolism and the self-destruction of cells--two biological processes central to health.
Related to videos 2570 and 2572.
Related to videos 2570 and 2572.
Gerhard Wagner, Harvard Medical School
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1315: Chromosomes before crossing over
1315: Chromosomes before crossing over
Duplicated pair of chromosomes lined up and ready to cross over.
Judith Stoffer
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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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6985: Fruit fly brain responds to adipokines
6985: Fruit fly brain responds to adipokines
Drosophila adult brain showing that an adipokine (fat hormone) generates a response from neurons (aqua) and regulates insulin-producing neurons (red).
Related to images 6982, 6983, and 6984.
Related to images 6982, 6983, and 6984.
Akhila Rajan, Fred Hutchinson Cancer Center
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2400: Pig trypsin (1)
2400: Pig trypsin (1)
A crystal of porcine trypsin protein created for X-ray crystallography, which can reveal detailed, three-dimensional protein structures.
Alex McPherson, University of California, Irvine
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3491: Kinesin moves cellular cargo
3491: Kinesin moves cellular cargo
A protein called kinesin (blue) is in charge of moving cargo around inside cells and helping them divide. It's powered by biological fuel called ATP (bright yellow) as it scoots along tube-like cellular tracks called microtubules (gray).
Charles Sindelar, Yale University
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3419: X-ray co-crystal structure of Src kinase bound to a DNA-templated macrocycle inhibitor 7
3419: X-ray co-crystal structure of Src kinase bound to a DNA-templated macrocycle inhibitor 7
X-ray co-crystal structure of Src kinase bound to a DNA-templated macrocycle inhibitor. Related to images 3413, 3414, 3415, 3416, 3417, and 3418.
Markus A. Seeliger, Stony Brook University Medical School and David R. Liu, Harvard University
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6793: Yeast cells with endocytic actin patches
6793: Yeast cells with endocytic actin patches
Yeast cells with endocytic actin patches (green). These patches help cells take in outside material. When a cell is in interphase, patches concentrate at its ends. During later stages of cell division, patches move to where the cell splits. This image was captured using wide-field microscopy with deconvolution.
Related to images 6791, 6792, 6794, 6797, 6798, and videos 6795 and 6796.
Related to images 6791, 6792, 6794, 6797, 6798, and videos 6795 and 6796.
Alaina Willet, Kathy Gould’s lab, Vanderbilt University.
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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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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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5759: TEM cross-section of C. elegans (roundworm)
5759: TEM cross-section of C. elegans (roundworm)
The worm Caenorhabditis elegans is a popular laboratory animal because its small size and fairly simple body make it easy to study. Scientists use this small worm to answer many research questions in developmental biology, neurobiology, and genetics. This image, which was taken with transmission electron microscopy (TEM), shows a cross-section through C. elegans, revealing various internal structures.
The image is from a figure in an article published in the journal eLife. There is an annotated version of this graphic at 5760.
The image is from a figure in an article published in the journal eLife. There is an annotated version of this graphic at 5760.
Piali Sengupta, Brandeis University
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2782: Disease-susceptible Arabidopsis leaf
2782: Disease-susceptible Arabidopsis leaf
This is a magnified view of an Arabidopsis thaliana leaf after several days of infection with the pathogen Hyaloperonospora arabidopsidis. The pathogen's blue hyphae grow throughout the leaf. On the leaf's edges, stalk-like structures called sporangiophores are beginning to mature and will release the pathogen's spores. Inside the leaf, the large, deep blue spots are structures called oopsorangia, also full of spores. Compare this response to that shown in Image 2781. Jeff Dangl has been funded by NIGMS to study the interactions between pathogens and hosts that allow or suppress infection.
Jeff Dangl, University of North Carolina, Chapel Hill
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2484: RNA Polymerase II
2484: RNA Polymerase II
NIGMS-funded researchers led by Roger Kornberg solved the structure of RNA polymerase II. This is the enzyme in mammalian cells that catalyzes the transcription of DNA into messenger RNA, the molecule that in turn dictates the order of amino acids in proteins. For his work on the mechanisms of mammalian transcription, Kornberg received the Nobel Prize in Chemistry in 2006.
David Bushnell, Ken Westover and Roger Kornberg, Stanford University
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3724: Snowflake DNA origami
3724: Snowflake DNA origami
An atomic force microscopy image shows DNA folded into an intricate, computer-designed structure. The image is featured on Biomedical Beat blog post Cool Images: A Holiday-Themed Collection. For more background on DNA origami, see Cool Image: DNA Origami. See also related image 3690.
Hao Yan, Arizona State University
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2545: Meiosis illustration
2545: Meiosis illustration
Meiosis is the process whereby a cell reduces its chromosomes from diploid to haploid in creating eggs or sperm. See image 2546 for a labeled version of this illustration. Featured in The New Genetics.
Crabtree + Company
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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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3520: HeLa cells
3520: HeLa cells
Multiphoton fluorescence image of HeLa cells with cytoskeletal microtubules (magenta) and DNA (cyan). Nikon RTS2000MP custom laser scanning microscope. See related images 3518, 3519, 3521, 3522.
National Center for Microscopy and Imaging Research (NCMIR)
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6548: Partial Model of a Cilium’s Doublet Microtubule
6548: Partial Model of a Cilium’s Doublet Microtubule
Cilia (cilium in singular) are complex molecular machines found on many of our cells. One component of cilia is the doublet microtubule, a major part of cilia’s skeletons that give them support and shape. This animated image is a partial model of a doublet microtubule’s structure based on cryo-electron microscopy images. Video can be found here 6549.
Brown Lab, Harvard Medical School and Veronica Falconieri Hays.
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