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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.
6486: CRISPR Illustration Frame 2
6486: CRISPR Illustration Frame 2
This illustration shows, in simplified terms, how the CRISPR-Cas9 system can be used as a gene-editing tool. The CRISPR system has two components joined together: a finely tuned targeting device (a small strand of RNA programmed to look for a specific DNA sequence) and a strong cutting device (an enzyme called Cas9 that can cut through a double strand of DNA). In this frame (2 of 4), the CRISPR machine locates the target DNA sequence once inserted into a cell.
For an explanation and overview of the CRISPR-Cas9 system, see the iBiology video, and find the full CRIPSR illustration here.
For an explanation and overview of the CRISPR-Cas9 system, see the iBiology video, and find the full CRIPSR illustration here.
National Institute of General Medical Sciences.
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3375: Electrostatic map of the adeno-associated virus with scale
3375: Electrostatic map of the adeno-associated virus with scale
The new highly efficient parallelized DelPhi software was used to calculate the potential map distribution of an entire virus, the adeno-associated virus, which is made up of more than 484,000 atoms. Despite the relatively large dimension of this biological system, resulting in 815x815x815 mesh points, the parallelized DelPhi, utilizing 100 CPUs, completed the calculations within less than three minutes. Related to image 3374.
Emil Alexov, Clemson University
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2320: Mapping disease spread
2320: Mapping disease spread
How far and fast an infectious disease spreads across a community depends on many factors, including transportation. These U.S. maps, developed as part of an international study to simulate and analyze disease spread, chart daily commuting patterns. They show where commuters live (top) and where they travel for work (bottom). Green represents the fewest number of people whereas orange, brown, and white depict the most. Such information enables researchers and policymakers to visualize how an outbreak in one area can spread quickly across a geographic region.
David Chrest, RTI International
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7014: Flagellated bacterial cells
7014: Flagellated bacterial cells
Vibrio fischeri (2 mm in length) is the exclusive symbiotic partner of the Hawaiian bobtail squid, Euprymna scolopes. After this bacterium uses its flagella to swim from the seawater into the light organ of a newly hatched juvenile, it colonizes the host and loses the appendages. This image was taken using a scanning electron microscope.
Margaret J. McFall-Ngai, Carnegie Institution for Science/California Institute of Technology, and Edward G. Ruby, California Institute of Technology.
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1282: Lysosomes
1282: Lysosomes
Lysosomes have powerful enzymes and acids to digest and recycle cell materials.
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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2752: Bacterial spore
2752: Bacterial spore
A spore from the bacterium Bacillus subtilis shows four outer layers that protect the cell from harsh environmental conditions.
Patrick Eichenberger, New York University
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2405: Rabbit GPDA
2405: Rabbit GPDA
A crystal of rabbit GPDA protein created for X-ray crystallography, which can reveal detailed, three-dimensional protein structures.
Alex McPherson, University of California, Irvine
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6661: Zebrafish embryo showing vasculature
6661: Zebrafish embryo showing vasculature
A zebrafish embryo. The blue areas are cell bodies, the green lines are blood vessels, and the red glow is blood. This image was created by stitching together five individual images captured with a hyperspectral multipoint confocal fluorescence microscope that was developed at the Eliceiri Lab.
Kevin Eliceiri, University of Wisconsin-Madison.
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3678: STORM image of axonal cytoskeleton
3678: STORM image of axonal cytoskeleton
This image shows the long, branched structures (axons) of nerve cells. Running horizontally across the middle of the photo is an axon wrapped in rings made of actin protein (green), which plays important roles in nerve cells. The image was captured with a powerful microscopy technique that allows scientists to see single molecules in living cells in real time. The technique is called stochastic optical reconstruction microscopy (STORM). It is based on technology so revolutionary that its developers earned the 2014 Nobel Prize in Chemistry. More information about this image can be found in: K. Xu, G. Zhong, X. Zhuang. Actin, spectrin and associated proteins form a periodic cytoskeleton structure in axons. Science 339, 452-456 (2013).
Xiaowei Zhuang Laboratory, Howard Hughes Medical Institute, Harvard University
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2395: Fungal lipase (1)
2395: Fungal lipase (1)
Crystals of fungal lipase protein created for X-ray crystallography, which can reveal detailed, three-dimensional protein structures.
Alex McPherson, University of California, Irvine
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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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3432: Mouse mammary cells lacking anti-cancer protein
3432: Mouse mammary cells lacking anti-cancer protein
Shortly after a pregnant woman gives birth, her breasts start to secrete milk. This process is triggered by hormonal and genetic cues, including the protein Elf5. Scientists discovered that Elf5 also has another job--it staves off cancer. Early in the development of breast cancer, human breast cells often lose Elf5 proteins. Cells without Elf5 change shape and spread readily--properties associated with metastasis. This image shows cells in the mouse mammary gland that are lacking Elf5, leading to the overproduction of other proteins (red) that increase the likelihood of metastasis.
Nature Cell Biology, November 2012, Volume 14 No 11 pp1113-1231
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6534: Mosaicism in C. elegans (White Background)
6534: Mosaicism in C. elegans (White Background)
In the worm C. elegans, double-stranded RNA made in neurons can silence matching genes in a variety of cell types through the transport of RNA between cells. The head region of three worms that were genetically modified to express a fluorescent protein were imaged and the images were color-coded based on depth. The worm on the left lacks neuronal double-stranded RNA and thus every cell is fluorescent. In the middle worm, the expression of the fluorescent protein is silenced by neuronal double-stranded RNA and thus most cells are not fluorescent. The worm on the right lacks an enzyme that amplifies RNA for silencing. Surprisingly, the identities of the cells that depend on this enzyme for gene silencing are unpredictable. As a result, worms of identical genotype are nevertheless random mosaics for how the function of gene silencing is carried out. For more, see journal article and press release. Related to image 6532.
Snusha Ravikumar, Ph.D., University of Maryland, College Park, and Antony M. Jose, Ph.D., University of Maryland, College Park
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1089: Natcher Building 09
1089: Natcher Building 09
NIGMS staff are located in the Natcher Building on the NIH campus.
Alisa Machalek, National Institute of General Medical Sciences
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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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2323: Motion in the brain
2323: Motion in the brain
Amid a network of blood vessels and star-shaped support cells, neurons in the brain signal each other. The mists of color show the flow of important molecules like glucose and oxygen. This image is a snapshot from a 52-second simulation created by an animation artist. Such visualizations make biological processes more accessible and easier to understand.
Kim Hager and Neal Prakash, University of California, Los Angeles
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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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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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2540: Chromosome inside nucleus (with labels)
2540: Chromosome inside nucleus (with labels)
The long, stringy DNA that makes up genes is spooled within chromosomes inside the nucleus of a cell. (Note that a gene would actually be a much longer stretch of DNA than what is shown here.) See image 2539 for an unlabeled version of this illustration. Featured in The New Genetics.
Crabtree + Company
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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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3525: Bacillus anthracis being killed
3525: Bacillus anthracis being killed
Bacillus anthracis (anthrax) cells being killed by a fluorescent trans-translation inhibitor, which disrupts bacterial protein synthesis. The inhibitor is naturally fluorescent and looks blue when it is excited by ultraviolet light in the microscope. This is a color version of Image 3481.
Kenneth Keiler, Penn State University
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1287: Mitochondria
1287: Mitochondria
Bean-shaped mitochondria are cells' power plants. These organelles have their own DNA and replicate independently. The highly folded inner membranes are the site of energy generation.
Judith Stoffer
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1092: Yeast cell
1092: Yeast cell
A whole yeast (Saccharomyces cerevisiae) cell viewed by X-ray microscopy. Inside, the nucleus and a large vacuole (red) are visible.
Carolyn Larabell, University of California, San Francisco and the Lawrence Berkeley National Laboratory
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3571: HIV-1 virus in the colon
3571: HIV-1 virus in the colon
A tomographic reconstruction of the colon shows the location of large pools of HIV-1 virus particles (in blue) located in the spaces between adjacent cells. The purple objects within each sphere represent the conical cores that are one of the structural hallmarks of the HIV virus.
Mark Ladinsky, California Institute of Technology
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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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2355: Nicotinic acid phosphoribosyltransferase
2355: Nicotinic acid phosphoribosyltransferase
Model of the enzyme nicotinic acid phosphoribosyltransferase. This enzyme, from the archaebacterium, Pyrococcus furiosus, is expected to be structurally similar to a clinically important human protein called B-cell colony enhancing factor based on amino acid sequence similarities and structure prediction methods. The structure consists of identical protein subunits, each shown in a different color, arranged in a ring.
Berkeley Structural Genomics Center, PSI
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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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3332: Polarized cells- 01
3332: Polarized cells- 01
Cells move forward with lamellipodia and filopodia supported by networks and bundles of actin filaments. Proper, controlled cell movement is a complex process. Recent research has shown that an actin-polymerizing factor called the Arp2/3 complex is the key component of the actin polymerization engine that drives amoeboid cell motility. ARPC3, a component of the Arp2/3 complex, plays a critical role in actin nucleation. In this photo, the ARPC3+/+ fibroblast cells were fixed and stained with Alexa 546 phalloidin for F-actin (red) and DAPI to visualize the nucleus (blue). ARPC3+/+ fibroblast cells with lamellipodia leading edge. Related to images 3328, 3329, 3330, 3331, and 3333.
Rong Li and Praveen Suraneni, Stowers Institute for Medical Research
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2315: Fly cells live
2315: Fly cells live
If a picture is worth a thousand words, what's a movie worth? For researchers studying cell migration, a "documentary" of fruit fly cells (bright green) traversing an egg chamber could answer longstanding questions about cell movement. Historically, researchers have been unable to watch this cell migration unfold in living ovarian tissue in real time. But by developing a culture medium that allows fly eggs to survive outside their ovarian homes, scientists can observe the nuances of cell migration as it happens. Such details may shed light on how immune cells move to a wound and why cancer cells spread to other sites. See 3594 for still image.
Denise Montell, Johns Hopkins 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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2299: 2-D NMR
2299: 2-D NMR
A two-dimensional NMR spectrum of a protein, in this case a 2D 1H-15N HSQC NMR spectrum of a 228 amino acid DNA/RNA-binding protein.
Dr. Xiaolian Gao's laboratory at the University of Houston
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3619: String-like Ebola virus peeling off an infected cell
3619: String-like Ebola virus peeling off an infected cell
After multiplying inside a host cell, the stringlike Ebola virus is emerging to infect more cells. Ebola is a rare, often fatal disease that occurs primarily in tropical regions of sub-Saharan Africa. The virus is believed to spread to humans through contact with wild animals, especially fruit bats. It can be transmitted between one person and another through bodily fluids.
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.
Heinz Feldmann, Peter Jahrling, Elizabeth Fischer and Anita Mora, National Institute of Allergy and Infectious Diseases, National Institutes of Health
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1166: Leptospira bacteria
1166: Leptospira bacteria
Leptospira, shown here in green, is a type (genus) of elongated, spiral-shaped bacteria. Infection can cause Weil's disease, a kind of jaundice, in humans.
Tina Weatherby Carvalho, University of Hawaii at Manoa
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3391: Protein folding video
3391: Protein folding video
Proteins are long chains of amino acids. Each protein has a unique amino acid sequence. It is still a mystery how a protein folds into the proper shape based on its sequence. Scientists hope that one day they can "watch" this folding process for any given protein. The dream has been realized, at least partially, through the use of computer simulation.
Theoretical and Computational Biophysics Group
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2794: Anti-tumor drug ecteinascidin 743 (ET-743), structure without hydrogens 01
2794: Anti-tumor drug ecteinascidin 743 (ET-743), structure without hydrogens 01
Ecteinascidin 743 (ET-743, brand name Yondelis), was discovered and isolated from a sea squirt, Ecteinascidia turbinata, by NIGMS grantee Kenneth Rinehart at the University of Illinois. It was synthesized by NIGMS grantees E.J. Corey and later by Samuel Danishefsky. Multiple versions of this structure are available as entries 2790-2797.
Timothy Jamison, Massachusetts Institute of Technology
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2508: Building blocks and folding of proteins
2508: Building blocks and folding of proteins
Proteins are made of amino acids hooked end-to-end like beads on a necklace. To become active, proteins must twist and fold into their final, or "native," conformation. A protein's final shape enables it to accomplish its function. Featured in The Structures of Life.
Crabtree + Company
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