The light organ (~0.5 mm across) of a juvenile Hawaiian bobtail squid, Euprymna scolopes, stained blue. The two pairs of ciliated appendages, or “arms,” on the sides of the organ move Vibrio fischeri bacterial cells closer to the two sets of three pores at the base of the arms that each lead to an interior crypt. This image was taken using a confocal fluorescence microscope.

Related to images 7017, 7018, 7019, and 7020.

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

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.

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), Arp2 (green), and DAPI to visualize the nucleus (blue). Arp2, a subunit of the Arp2/3 complex, is localized at the lamellipodia leading edge of ARPC3+/+ fibroblast cells. Related to images 3329, 3330, 3331, 3332, and 3333.

These cells get their name from the hairlike structures that extend from them into the fluid-filled tube of the inner ear. When sound reaches the ear, the hairs bend and the cells convert this movement into signals that are relayed to the brain. When we pump up the music in our cars or join tens of thousands of cheering fans at a football stadium, the noise can make the hairs bend so far that they actually break, resulting in long-term hearing loss.

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

CCD-1 is an enzyme produced by the bacterium Clostridioides difficile that helps it resist antibiotics. Researchers crystallized complexes where a CCD-1 molecule and a molecule of the antibiotic cefotaxime were bound together. Then, they shot X-rays at the complexes to determine their structure—a process known as X-ray crystallography. This image shows the X-ray diffraction pattern of a complex.

Related to images 6764, 6766, and 6767.

Inside the fertilized egg cell of a fruit fly, we see a type of myosin (related to the protein that helps muscles contract) made to glow by attaching a fluorescent protein. After fertilization, the myosin proteins are distributed relatively evenly near the surface of the embryo. The proteins temporarily vanish each time the cells' nuclei--initially buried deep in the cytoplasm--divide. When the multiplying nuclei move to the surface, they shift the myosin, producing darkened holes. The glowing myosin proteins then gather, contract, and start separating the nuclei into their own compartments.

Yeast cells with the protein Fimbrin Fim1 shown in magenta. This protein plays a role in cell division. This image was captured using wide-field microscopy with deconvolution.

Related to images 6791, 6792, 6793, 6797, 6798, and videos 6795 and 6796.

This image shows the extracellular matrix (ECM) on the surface of a soleus (lower calf) muscle in light brown and blood vessels in pink. Near the bottom of the photo, a vessel is opened up to reveal red blood cells. Scientists know less about the ECM in muscle than in other tissues, but it's increasingly clear that the ECM is critical to muscle function, and disruption of the ECM has been associated with many muscle disorders. The ECM in muscles stores and releases growth factors, suggesting that it might play a role in cellular communication.

Insect brains, like the honeybee brain shown here, are very different in shape from human brains. Despite that, bee and human brains have a lot in common, including many of the genes and neurochemicals they rely on in order to function. The bright-green spots in this image indicate the presence of tyrosine hydroxylase, an enzyme that allows the brain to produce dopamine. Dopamine is involved in many important functions, such as the ability to experience pleasure. This image was captured using confocal microscopy.

Sulfite oxidase is an enzyme that is essential for normal neurological development in children. This video shows the active site of the enzyme and its molybdenum cofactor visible as a faint ball-and-stick representation buried within the protein. The positively charged channel (blue) at the active site contains a chloride ion (green) and three water molecules (red). As the protein oscillates, one can see directly down the positively charged channel. At the bottom is the molybdenum atom of the active site (light blue) and its oxo group (red) that is transferred to sulfite to form sulfate in the catalytic reaction.

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.

Trajectories of single molecule labeled cell surface receptors. This is an example of NIH-supported research on single-cell analysis. Related to 2798 , 2799, 2800, 2802 and 2803.

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.

A zebrafish embryo showing its natural colors. Zebrafish have see-through eggs and embryos, making them ideal research organisms for studying the earliest stages of development. This image was taken in transmitted light under a polychromatic polarizing microscope.

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

Some children are born with a mutation in a regulatory site on this enzyme that causes them to over-secrete insulin when they consume protein. We found that a compound from green tea (shown in the stick figure and by the yellow spheres on the enzyme) is able to block this hyperactivity when given to animals with this disorder.

This Petri dish contains microscopic roundworms called Caenorhabditis elegans. Researchers used these particular worms to study how C. elegans senses the color of light in its environment.

Model of aspartoacylase, a human enzyme involved in brain metabolism.

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.

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.

This photo shows a Varian Unity Inova 900 MHz, 21.1 T standard bore magnet Nuclear Magnetic Resonnance (NMR) spectrometer. NMR spectroscopy provides data used to determine the structures of proteins in solution, rather than in crystal form, as in X-ray crystallography. The technique is limited to smaller proteins or protein fragments in a high throughput approach.

The human body keeps time with a master clock called the suprachiasmatic nucleus or SCN. Situated inside the brain, it's a tiny sliver of tissue about the size of a grain of rice, located behind the eyes. It sits quite close to the optic nerve, which controls vision, and this means that the SCN "clock" can keep track of day and night. The SCN helps control sleep and maintains our circadian rhythm--the regular, 24-hour (or so) cycle of ups and downs in our bodily processes such as hormone levels, blood pressure, and sleepiness. The SCN regulates our circadian rhythm by coordinating the actions of billions of miniature "clocks" throughout the body. These aren't actually clocks, but rather are ensembles of genes inside clusters of cells that switch on and off in a regular, 24-hour (or so) cycle in our physiological day.

Two mouse fibroblasts, one of the most common types of cells in mammalian connective tissue. They play a key role in wound healing and tissue repair. This image was captured using structured illumination microscopy.

Disassembly of vasculature in kdr:GFP frogs following addition of 250 µM TBZ. Related to images 3404 and 3505.

Zika virus is shown in cross section at center left. On the outside, it includes envelope protein (red) and membrane protein (magenta) embedded in a lipid membrane (light purple). Inside, the RNA genome (yellow) is associated with capsid proteins (orange). The viruses are shown interacting with receptors on the cell surface (green) and are surrounded by blood plasma molecules at the top.

A crawling cell with DNA shown in blue and actin filaments, which are a major component of the cytoskeleton, visible in pink. Actin filaments help enable cells to crawl. This image was captured using structured illumination microscopy.

Fruit flies are a common model organism for basic medical research.

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.

Human cells with the gene that codes for the protein FIT2 deleted. After an experimental intervention, they are expressing a nonfunctional version of FIT2, shown in green. The lack of functional FIT2 affected the structure of the endoplasmic reticulum (ER), and the nonfunctional protein clustered in ER membrane aggregates, seen as large bright-green spots. Lipid droplets are shown in red, and the nucleus is visible in gray. This image was captured using a confocal microscope. Related to image 6773.

Model of a protein, antigen 85B, that is the most abundant protein exported by Mycobacterium tuberculosis, which causes most cases of tuberculosis. Antigen 85B is involved in building the bacterial cell wall and is an attractive drug target. Based on its structure, scientists have suggested a new class of antituberculous drugs.

This network map shows molecular interactions (yellow) associated with a congenital condition that causes heart arrhythmias and the targets for drugs that alter these interactions (red and blue).

An image of the area of the mouse brain that serves as the 'master clock,' which houses the brain's time-keeping neurons. The nuclei of the clock cells are shown in blue. A small molecule called VIP, shown in green, enables neurons in the central clock in the mammalian brain to synchronize.

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.

The glial cells (black dots) and nerve cells (brown bands) in this developing fruit fly nerve cord formed normally despite the absence of the SPITZ protein, which blocks their impending suicide. The HID protein, which triggers suicide, is also lacking in this embryo.

The "epigenetic code" controls gene activity with chemical tags that mark DNA (purple diamonds) and the "tails" of histone proteins (purple triangles). These markings help determine whether genes will be transcribed by RNA polymerase. Genes hidden from access to RNA polymerase are not expressed. See image 2562 for an unlabeled version of this illustration. Featured in The New Genetics.

Embryonic stem cells store pre-activated Bax (red) in the Golgi, near the nucleus (blue). Featured in the June 21, 2012, issue of Biomedical Beat.

The green spots in this image are clumps of protein inside yeast cells that are deficient in both zinc and a protein called Tsa1 that prevents clumping. Protein clumping plays a role in many diseases, including Parkinson's and Alzheimer's, where proteins clump together in the brain. Zinc deficiency within a cell can cause proteins to mis-fold and eventually clump together. Normally, in yeast, Tsa1 codes for so-called "chaperone proteins" which help proteins in stressed cells, such as those with a zinc deficiency, fold correctly. The research behind this image was published in 2013 in the Journal of Biological Chemistry.

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.

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 3725 and 3675.

Multicellular yeast called snowflake yeast that researchers created through many generations of directed evolution from unicellular yeast. Here, the researchers visualized nuclei in orange to help them study changes in how the yeast cells divided. Cell walls are shown in blue. This image was captured using spinning disk confocal microscopy.

Related to images 6969 and 6970.

Model of a protein involved in cell division from Mycoplasma pneumoniae. This model, based on X-ray crystallography, revealed a structural domain not seen before. The protein is thought to be involved in cell division and cell wall biosynthesis.

Many disease-causing microbes manipulate their host’s metabolism and cells for their own ends. Microsporidia—which are parasites closely related to fungi—infect and multiply inside animal cells, and take the rearranging of cells’ interiors to a new level. They reprogram animal cells such that the cells start to fuse, causing them to form long, continuous tubes. As shown in this image of the roundworm Caenorhabditis elegans, microsporidia (dark oval shapes) invaded the worm’s gut cells (long tube; the cell nuclei are shown in red) and have instructed the cells to merge. The cell fusion enables the microsporidia to thrive and propagate in the expanded space. Scientists study microsporidia in worms to gain more insight into how these parasites manipulate their host cells. This knowledge might help researchers devise strategies to prevent or treat infections with microsporidia.

For more on the research into microsporidia, see this news release from the University of California San Diego. Related to images 5777 and 5779.

X-ray crystallography allows researchers to see structures too small to be seen by even the most powerful microscopes. To visualize the arrangement of atoms within molecules, researchers can use the diffraction patterns obtained by passing X-ray beams through crystals of the molecule. This is a common way for solving the structures of proteins. See image 2511 for an unlabeled version of this illustration. Featured in The Structures of Life.

Professor Marc Zimmer's family pets, including these fish, glow in the dark in response to blue light. Featured in the September 2009 issue of Findings.

This image shows neonatal mouse heart cells. These cells were grown in the lab on a chip that aligns the cells in a way that mimics what is normally seen in the body. Green shows the protein N-cadherin, which indicates normal connections between cells. Red indicates the muscle protein actin, and blue indicates the cell nuclei. The work shown here was part of a study attempting to grow heart tissue in the lab to repair damage after a heart attack. Image and caption information courtesy of the California Institute for Regenerative Medicine. Related to images 3281 and 3283.

A light microscope image of cells from the endosperm of an African globe lily (Scadoxus katherinae). This is one frame of a time-lapse sequence that shows cell division in action. The lily is considered a good organism for studying cell division because its chromosomes are much thicker and easier to see than human ones. Staining shows microtubules in red and chromosomes in blue. Here, two cells have formed after a round of mitosis.

Related to images 1010, 1011, 1012, 1013, 1014, 1015, 1016, 1017, 1018, and 1021.

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.

A knotted protein from an archaebacterium called Methanobacterium thermoautotrophicam. This organism breaks down waste products and produces methane gas. Protein folding theory previously held that forming a knot was beyond the ability of a protein, but this structure, determined at Argonne's Structural Biology Center, proves differently. Researchers theorize that this knot stabilizes the amino acid subunits of the protein.