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.

A crystal of RNase A protein created for X-ray crystallography, which can reveal detailed, three-dimensional protein structures.

A crystal of hen egg lysozyme protein created for X-ray crystallography, which can reveal detailed, three-dimensional protein structures.

Arranging exons in different patterns, called alternative splicing, enables cells to make different proteins from a single gene. Featured in The New Genetics.

See image 2552 for an unlabeled version of this illustration.

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.

Circadian rhythms are physical, mental, and behavioral changes that follow a 24-hour cycle. Typical circadian rhythms lead to high energy during the middle of the day (10 a.m. to 1 p.m.) and an afternoon slump. At night, circadian rhythms cause the hormone melatonin to rise, making a person sleepy.

Learn more in NIGMS’ circadian rhythms featured topics page.

See 6612 for the Spanish version of this infographic.

A replica of a human retina grown from stem cells. It shows rod photoreceptors (nerve cells responsible for dark vision) in green and red/green cones (nerve cells responsible for red and green color vision) in red. The cell nuclei are stained blue. This image was captured using a confocal microscope.

Two adult fruit flies (Drosophila)

This image shows two components of the cytoskeleton, microtubules (green) and actin filaments (red), in an endothelial cell derived from a cow lung. The cystoskeleton provides the cell with an inner framework and enables it to move and change shape.

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.

A global "map of the protein structure universe" indicating the positions of specific proteins. The preponderance of small, less-structured proteins near the origin, with the more highly structured, large proteins towards the ends of the axes, may suggest the evolution of protein structures.

This illustration shows, in simplified terms, how the CRISPR-Cas9 system can be used as a gene-editing tool. This is the fifthframe in a series of five. 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). For an explanation and overview of the CRISPR-Cas9 system, see the NIGMS Biomedical Beat blog entry, Field Focus: Precision Gene Editing with CRISPR and the iBiology video, Genome Engineering with CRISPR-Cas9: Birth of a Breakthrough Technology.

Learn about basic science, sometimes called “pure” or “fundamental” science, and how it contributes to the development of medical treatments. Discover more resources from NIGMS’ Pathways collaboration with Scholastic. View the video on YouTube for closed captioning.

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.

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.

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

This image shows a computer-generated, three-dimensional map of the rotavirus structure. This virus infects humans and other animals and causes severe diarrhea in infants and young children. By the age of five, almost every child in the world has been infected with this virus at least once. Scientists have found a vaccine against rotavirus, so in the United States there are very few fatalities, but in developing countries and in places where the vaccine is unavailable, this virus is responsible for more than 200,000 deaths each year.

The rotavirus comprises three layers: the outer, middle and inner layers. On infection, the outer layer is removed, leaving behind a "double-layered particle." Researchers have studied the structure of this double-layered particle with a transmission electron microscope. Many images of the virus at a magnification of ~50,000x were acquired, and computational analysis was used to combine the individual particle images into a three-dimensional reconstruction.

The image was rendered by Melody Campbell (PhD student at TSRI). Work that led to the 3D map was published in Campbell et al. Movies of ice-embedded particles enhance resolution in electron cryo-microscopy. Structure. 2012;20(11):1823-8. PMCID: PMC3510009.

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

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. Cell nuclei are in blue. Red and orange mark hair follicle stem cells (hair follicle stem cells activate to cause hair regrowth, which indicates healing). See more information in the article in Science.

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

A crystal of Bence Jones protein created for X-ray crystallography, which can reveal detailed, three-dimensional protein structures.

Molecular biologists are increasingly relying on bioinformatics software to visualize molecular interaction networks and to integrate these networks with data such as gene expression profiles. Related to 2749.

This is a super-resolution light microscope image taken by Hiro Hakozaki and Masa Hoshijima of NCMIR. The image contains highlighted calcium channels in cardiac muscle using a technique called dSTORM. The microscope used in the NCMIR lab was built by Hiro Hakozaki.

The nuclei stained green highlight human embryonic stem cells grown under controlled conditions in a laboratory. Blue represents the DNA of surrounding, supportive feeder cells. Image and caption information courtesy of the California Institute for Regenerative Medicine. See related image 3724.

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.

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 2515 for other versions of this illustration. Featured in The Structures of Life.

These yeast cells were exposed to a glucose (sugar) shortage. This caused the cells to compartmentalize HMGCR (green)—an enzyme involved in making cholesterol—to a patch on the nuclear envelope next to the vacuole/lysosome (purple). This process enhanced HMGCR activity and helped the yeast adapt to the glucose shortage. Researchers hope that understanding how yeast regulate cholesterol could ultimately lead to new ways to treat high cholesterol in people. This image was captured using a fluorescence microscope.

Human cells with the gene that codes for the protein FIT2 deleted. Green indicates an endoplasmic reticulum (ER) resident protein. The lack of FIT2 affected the structure of the ER and caused the resident protein to cluster in ER membrane aggregates, seen as large, bright-green spots. Red shows where the degradation of cell parts—called autophagy—is taking place, and the nucleus is visible in blue. This image was captured using a confocal microscope.

Jellyfish are especially good models for studying the evolution of embryonic tissue layers. Despite being primitive, jellyfish have a nervous system (stained green here) and musculature (red). Cell nuclei are stained blue. By studying how tissues are distributed in this simple organism, scientists can learn about the evolution of the shapes and features of diverse animals.

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

Fruit fly sperm cells glow bright green when they express the gene for green fluorescent protein (GFP).

Illustration of a sperm, the male reproductive cell.

The membrane that surrounds a cell is made up of proteins and lipids. Depending on the membrane's location and role in the body, lipids can make up anywhere from 20 to 80 percent of the membrane, with the remainder being proteins. Cholesterol (green), which is not found in plant cells, is a type of lipid that helps stiffen the membrane.

The nucleus of a degenerating human tendon cell, also known as a tenocyte. It has been color-coded based on the density of chromatin—a substance made up of DNA and proteins. Areas of low chromatin density are shown in blue, and areas of high chromatin density are shown in red. This image was captured using Stochastic Optical Reconstruction Microscopy (STORM).

Related to images 6887 and 6888.

A computer-generated sketch of a DNA origami folded into a flower-and-bird structure. See also related image 3690.

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.

Crystals of hen egg lysozyme protein created for X-ray crystallography, which can reveal detailed, three-dimensional protein structures.

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-in version 5767 of this illustration.

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.

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.

During development, a zebrafish embryo is transformed from a ball of cells into a recognizable body plan by sweeping convergence and extension cell movements. This process is called gastrulation. Each line in this video represents the movement of a single zebrafish embryo cell over the course of 3 hours. The video was created using time-lapse confocal microscopy. Related to image 6775.

Two healthy cells (bottom, left) enter into apoptosis (bottom, center) but spring back to life after a fatal toxin is removed (bottom, right; top).

As this cell was undergoing cell division, it was imaged with two microscopy techniques: differential interference contrast (DIC) and confocal. The DIC view appears in blue and shows the entire cell. The confocal view appears in pink and shows the chromosomes.

Model of a major secreted protein of unknown function, which is only found in mycobacteria, the class of bacteria that causes tuberculosis. Based on structural similarity, this protein may be involved in host-bacterial interactions.

The molecule on the left is an electrostatic potential map of the van der Waals surface of the transition state for human purine nucleoside phosphorylase. The colors indicate the electron density at any position of the molecule. Red indicates electron-rich regions with negative charge and blue indicates electron-poor regions with positive charge. The molecule on the right is called DADMe-ImmH. It is a chemically stable analogue of the transition state on the left. It binds to the enzyme millions of times tighter than the substrate. This inhibitor is in human clinical trials for treating patients with gout. This image appears in Figure 4, Schramm, V.L. (2011) Annu. Rev. Biochem. 80:703-732.

A crystal of bovine milk alpha-lactalbumin protein created for X-ray crystallography, which can reveal detailed, three-dimensional protein structures.

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.

A mouse's fat cells (red) are shown surrounded by a network of blood vessels (green). Fat cells store and release energy, protect organs and nerve tissues, insulate us from the cold, and help us absorb important vitamins.

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

DNA doesn't leave a fossil record in stone, the way bones do. Instead, the DNA code itself holds the best evidence for organisms' genetic history. Some of the most telling evidence about genetic history comes from retroviruses, the remnants of ancient viral infections.

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

In this image, recombinant probes known as FingRs (Fibronectin Intrabodies Generated by mRNA display) were expressed in a cortical neuron, where they attached fluorescent proteins to either PSD95 (green) or Gephyrin (red). PSD-95 is a marker for synaptic strength at excitatory postsynaptic sites, and Gephyrin plays a similar role at inhibitory postsynaptic sites. Thus, using FingRs it is possible to obtain a map of synaptic connections onto a particular neuron in a living cell in real time.

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 black-and-white version of Image 3525.