The incredible complexity of a mammalian eye (in this case from a mouse) is captured here. Each color represents a different type of cell. In total, there are nearly 70 different cell types, including the retina's many rings and the peach-colored muscle cells clustered on the left.

This image was part of the Life: Magnified exhibit that ran from June 3, 2014, to January 21, 2015, at Dulles International Airport.

Some nerve cells (neurons) in the brain keep track of the daily cycle. This time-keeping mechanism, called the circadian clock, is found in all animals including us. The circadian clock controls our daily activities such as sleep and wakefulness. Researchers are interested in finding the neuron circuits involved in this time keeping and how the information about daily time in the brain is relayed to the rest of the body. In this image of a brain of the fruit fly Drosophila the time-of-day information flowing through the brain has been visualized by staining the neurons involved: clock neurons (shown in blue) function as "pacemakers" by communicating with neurons that produce a short protein called leucokinin (LK) (red), which, in turn, relays the time signal to other neurons, called LK-R neurons (green). This signaling cascade set in motion by the pacemaker neurons helps synchronize the fly's daily activity with the 24-hour cycle. To learn more about what scientists have found out about circadian pacemaker neurons in the fruit fly see this news release by New York University. This work was featured in the Biomedical Beat blog post Cool Image: A Circadian Circuit.

Luciferase-based imaging enables visualization and quantification of internal organs and transplanted cells in live adult zebrafish. In this image, a cardiac muscle-restricted promoter drives firefly luciferase expression.
For imagery of both the lateral and overhead view go to 3556.
For imagery of the lateral view go to 3558.
For more information about the illumated area go to 3559.

Jon Lorsch at his swearing in as NIGMS director in August 2013. Also shown are Francis Collins, NIH Director, and Judith Greenberg, former NIGMS Acting Director.

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.

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.

For more information on this see, relapsing fever.

This image was part of the Life: Magnified exhibit that ran from June 3, 2014, to January 21, 2015, at Dulles International Airport.

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, two multivesicular bodies (with yellow membranes) contain tiny intralumenal vesicles (with a diameter of only 25 nanometers; shown in red) adjacent to the cell's vacuole (in orange).

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 microscopy photograph 5768 that was used to generate this illustration and a zoomed-out version 5769 of this illustration.

The brain sections are treated with fluorescent antibodies specific to a particular protein and visualized using serial electron microscopy (SEM).

Developing spermatids (precursors of mature sperm cells) begin as small, round cells and mature into long-tailed, tadpole-shaped ones. In the sperm cell's head is the cell nucleus; in its tail is the power to outswim thousands of competitors to fertilize an egg. As seen in this microscopy image, fruit fly spermatids start out as groups of interconnected cells. A small lipid molecule called PIP2 helps spermatids tell their heads from their tails. Here, PIP2 (red) marks the nuclei and a cell skeleton-building protein called tubulin (green) marks the tails. When PIP2 levels are too low, some spermatids get mixed up and grow with their heads at the wrong end. Because sperm development is similar across species, studies in fruit flies could help researchers understand male infertility in humans.

The G switch allows our bodies to respond rapidly to hormones. G proteins act like relay batons to pass messages from circulating hormones into cells. A hormone (red) encounters a receptor (blue) in the membrane of a cell. Next, a G protein (green) becomes activated and makes contact with the receptor to which the hormone is attached. Finally, the G protein passes the hormone's message to the cell by switching on a cell enzyme (purple) that triggers a response. See image 2536 and 2538 for other versions of this image. Featured in Medicines By Design.

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 2540 for a labeled version of this illustration. Featured in The New Genetics.

Hydra magnipapillata is an invertebrate animal used as a model organism to study developmental questions, for example the formation of the body axis.

The genetic code in DNA is transcribed into RNA, which is translated into proteins with specific sequences. During transcription, 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 2509 for an unlabeled version of this illustration.

Featured in The Structures of Life.

Xenopus laevis, the African clawed frog, has long been used as a model organism for studying embryonic development. The frog embryo on the left lacks the developmental factor Sizzled. A normal embryo is shown on the right.

Cross section of human skeletal muscle. Image taken with a confocal fluorescent light microscope.

Georgia Tech associate professor Hang Lu holds a microfluidic chip that is part of a system that uses artificial intelligence and cutting-edge image processing to automatically examine large number of nematodes used for genetic research.

The receptor is shown bound to an inverse agonist, doxepin.

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.

Stereo triplet of a sea urchin embryo stained to reveal actin filaments (orange) and microtubules (blue). This image is part of a series of images: 1047, 1048, 1049, 1050 and 1052.

A genetic disorder of the nervous system, neurofibromatosis causes tumors to form on nerves throughout the body, including a type of tumor called an optic nerve glioma that can result in childhood blindness. The image was used to demonstrate the unique imaging capabilities of one of our newest (at the time) laser scanning microscopes and is of a wildtype (normal) mouse retina in the optic fiber layer. This layer is responsible for relaying information from the retina to the brain and was fluorescently stained to reveal the distribution of glial cells (green), DNA and RNA in the cell bodies of the retinal ganglion neurons (orange) and their optic nerve fibers (red), and actin in endothelial cells surrounding a prominent branching blood vessel (blue). By studying the microscopic structure of normal and diseased retina and optic nerves, we hope to better understand the altered biology of the tissues in these tumors with the prospects of developing therapeutic interventions.

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.

Crystals of fungal lipase protein created for X-ray crystallography, which can reveal detailed, three-dimensional protein structures.

A sensor particle being engulfed by a macrophage—an immune cell—and encapsuled in a compartment called a phagosome. The phagosome then fuses with lysosomes—another type of compartment. The left video shows snowman-shaped sensor particles with fluorescent green nanoparticle “heads” and “bodies” colored red by Förster Resonance Energy Transfer (FRET)-donor fluorophores. The middle video visualizes light blue FRET signals that are only generated when the “snowman” sensor—the FRET-donor—fuses with the lysosomes, which are loaded with FRET-acceptors. The right video combines the other two. The videos were captured using epi-fluorescence microscopy.

More details can be found in the paper “Transport motility of phagosomes on actin and microtubules regulates timing and kinetics of their maturation” by Yu et al.

Scientists use nuclear magnetic spectroscopy (NMR) to determine the detailed, 3D structures of molecules.

Model of an enzyme, PanC, that is involved in the last step of vitamin B5 biosynthesis in Mycobacterium tuberculosis. PanC is essential for the growth of M. tuberculosis, which causes most cases of tuberculosis, and is therefore a potential drug target.

A protein called tubulin (green) accumulates in the center of a nucleus (outlined in pink) from an aging cell. Normally, this protein is kept out of the nucleus with the help of gatekeepers known as nuclear pore complexes. But NIGMS-funded researchers found that wear and tear to long-lived components of the complexes eventually lowers the gatekeepers' guard. As a result, cytoplasmic proteins like tubulin gain entry to the nucleus while proteins normally confined to the nucleus seep out. The work suggests that finding ways to stop the leakage could slow the cellular aging process and possibly lead to new therapies for age-related diseases.

This fiery image doesn’t come from inside a bubbling volcano. Instead, it shows animal cells caught in the act of making bubbles, or blebbing. Some cells regularly pinch off parts of their membranes to produce bubbles filled with a mix of proteins and fats. The bubbles (red) are called plasma-derived membrane vesicles, or PMVs, and can travel to other parts of the body where they may aid in cell-cell communication. The University of Texas, Austin, researchers responsible for this photo are exploring ways to use PMVs to deliver medicines to precise locations in the body.

This image, entered in the Biophysical Society’s 2017 Art of Science Image contest, used two-channel spinning disk confocal fluorescence microscopy. It was also featured in the NIH Director’s Blog in May 2017.

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.

Multiphoton fluorescence image of HeLa cells stained with the actin binding toxin phalloidin (red), microtubules (cyan) and cell nuclei (blue). Nikon RTS2000MP custom laser scanning microscope. See related images 3518, 3519, 3520, 3522.

Learn about how bacteria and viruses differ, how they each can make you sick, and how they can or cannot be treated. Discover more resources from NIGMS’ Pathways collaboration with Scholastic. View the video on YouTube for closed captioning.

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.

Enzymes convert substrates into products very quickly. See image 2521 for an unlabeled version of this illustration. Featured in The Chemistry of Health.

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.

In SARS-CoV-2, the virus that causes COVID-19, nucleocapsid is a complex molecule with many functional parts. One section folds into an RNA-binding domain, with a groove that grips a short segment of the viral genomic RNA. Another section folds into a dimerization domain that brings two nucleocapsid molecules together. The rest of the protein is intrinsically disordered, forming tails at each end of the protein chain and a flexible linker that connects the two structured domains. These disordered regions assist with RNA binding and orchestrate association of nucleocapsid dimers into larger assemblies that package the RNA in the small space inside virions. Nucleocapsid is in magenta and purple, and short RNA strands are in yellow.

Find these in the RCSB Protein Data Bank: RNA-binding domain (PDB entry 7ACT) and Dimerization domain (PDB entry 6WJI).

RNA interference or RNAi is a gene-silencing process in which double-stranded RNAs trigger the destruction of specific RNAs. See 2558 for an unlabeled version of this illustration. Featured in The New Genetics.

Irina Dementieva, a biochemist, and Youngchang Kim, a biophysicist and crystallographer, work with the first robot of its type in the U.S. to automate protein purification. The robot, which is housed in a refrigerator, is an integral part of the Midwest Structural Genomics Center's plan to automate the protein crystallography process.

NIGMS staff are located in the Natcher Building on the NIH campus.

Influenza A infects a host cell when hemagglutinin grips onto glycans on its surface. Neuraminidase, an enzyme that chews sugars, helps newly made virus particles detach so they can infect other cells. Related to 213. Featured in the March 2006, issue of Findings in "Viral Voyages."

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).

This graphic that resembles a firework was created from a picture of a fruit fly spermatid. This fruit fly spermatid recycles various molecules, including malformed or damaged proteins. Actin filaments (red) in the cell draw unwanted proteins toward a barrel-shaped structure called the proteasome (green clusters), which degrades the molecules into their basic parts for re-use.

Body organs such as the liver and kidneys process chemicals and toxins. These "target" organs are susceptible to damage caused by these substances. See image 2496 for an unlabeled version of this illustration.

2.5Å resolution reconstruction of rabbit muscle aldolase collected on a FEI/Thermo Fisher Titan Krios with energy filter and image corrector.

Actin gliding powered by myosin 1D. Note the counterclockwise motion of the gliding actin filaments.

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), mDia1 (green), and DAPI to visualize the nucleus (blue). mDia1 is localized at the lamellipodia of ARPC3+/+ fibroblast cells. Related to images 3328, 3329, 3331, 3332, and 3333.

Like a watch wrapped around a wrist, a special enzyme encircles the double helix to repair a broken strand of DNA. Without molecules that can mend such breaks, cells can malfunction, die, or become cancerous. Related to image 2330.

This image shows mouse fetal heart fibroblast cells. The muscle protein actin is stained red, and the cell nuclei are stained blue. The image was part of a study investigating stem cell-based approaches to repairing tissue damage after a heart attack. Image and caption information courtesy of the California Institute for Regenerative Medicine.

Yeast make bread, beer, and wine. And like us, yeast can reproduce sexually. A mother and father cell fuse and create one large cell that contains four offspring. When environmental conditions are favorable, the offspring are released, as shown here. Yeast are also a popular study subject for scientists. Research on yeast has yielded vast knowledge about basic cellular and molecular biology as well as about myriad human diseases, including colon cancer and various metabolic disorders.

This image was part of the Life: Magnified exhibit that ran from June 3, 2014, to January 21, 2015, at Dulles International Airport.

Luciferase-based imaging enables visualization and quantification of internal organs and transplanted cells in live adult zebrafish. This image shows how luciferase-based imaging could be used to visualize the heart for regeneration studies (left), or label all tissues for stem cell transplantation (right).
For imagery of both the lateral and overhead view go to 3556.
For imagery of the overhead view go to 3557.
For imagery of the lateral view go to 3558.

Serum albumin (SA) is the most abundant protein in the blood plasma of mammals. SA has a characteristic heart-shape structure and is a highly versatile protein. It helps maintain normal water levels in our tissues and carries almost half of all calcium ions in human blood. SA also transports some hormones, nutrients and metals throughout the bloodstream. Despite being very similar to our own SA, those from other animals can cause some mild allergies in people. Therefore, some scientists study SAs from humans and other mammals to learn more about what subtle structural or other differences cause immune responses in the body.

Related to entries 3744 and 3746

Scientists in Scotland were the first to clone an animal, this sheep named Dolly. She later gave birth to Bonnie, the lamb next to her.