In the determination of protein structures by X-ray crystallography, this unique soft (l = 2.29Å) X-ray source is used to collect anomalous scattering data from protein crystals containing light atoms such as sulfur, calcium, zinc and phosphorous. These data can be used to image the protein.

Researchers have created artificial cilia that wave like the real thing. Zvonimir Dogic and his Brandeis University colleagues combined just a few cilia proteins to create cilia that are able to wave and sweep material around--although more slowly and simply than real ones. The researchers are using the lab-made cilia to study how the structures coordinate their movements and what happens when they don't move properly. Featured in the August 18, 2011, issue of Biomedical Beat.

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.

Using an electrode, researchers apply an electrical pulse onto a piece of muscle tissue affected by Huntington's disease.

These time series show the heart rates of four different individuals. Automakers use steel scraps to build cars, construction companies repurpose tires to lay running tracks, and now scientists are reusing previously discarded medical data to better understand our complex physiology. Through a website called PhysioNet developed in part by Beth Israel Deaconess Medical Center cardiologist Ary Goldberger, scientists can access complete physiologic recordings, such as heart rate, respiration, brain activity and gait. They then can use free software to analyze the data and find patterns in it. The patterns could ultimately help health care professionals diagnose and treat health conditions like congestive heart failure, sleeping disorders, epilepsy and walking problems. PhysioNet is supported by NIH's National Institute of Biomedical Imaging and Bioengineering as well as by NIGMS.

The Center for Eukaryotic Structural Genomics protein purification facility is responsible for purifying all recombinant proteins produced by the center. The facility performs several purification steps, monitors the quality of the processes, and stores information about the biochemical properties of the purified proteins in the facility database.

An anchor cell (red) pushes through the basement membrane (green) that surrounds it. Some cells are able to push through the tough basement barrier to carry out important tasks--and so can cancer cells, when they spread from one part of the body to another. No one has been able to recreate basement membranes in the lab and they're hard to study in humans, so Duke University researchers turned to the simple worm C. elegans. The researchers identified two molecules that help certain cells orient themselves toward and then punch through the worm's basement membrane. Studying these molecules and the genes that control them could deepen our understanding of cancer spread.

Mitosis creates cells, and apoptosis kills them. The processes often work together to keep us healthy.

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

Bacterial biofilms are tightly knit communities of bacterial cells growing on, for example, solid surfaces, such as in water pipes or on teeth. Here, cells of the bacterium Bacillus subtilis have formed a biofilm in a laboratory culture. Researchers have discovered that the bacterial cells in a biofilm communicate with each other through electrical signals via specialized potassium ion channels to share resources, such as nutrients, with each other. This insight may help scientists to improve sanitation systems to prevent biofilms, which often resist common treatments, from forming and to develop better medicines to combat bacterial infections. See the Biomedical Beat blog post Bacterial Biofilms: A Charged Environment for more information.

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.

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

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 3375.

These smooth muscle cells were derived from human embryonic stem cells. The nuclei are stained blue, and the proteins of the cytoskeleton are stained green. Image and caption information courtesy of the California Institute for Regenerative Medicine.

Rendering of the surface of an endothelial cell; membrane curvature is color coded. This is an example of NIH-supported research on single-cell analysis. Related to 2798 , 2799, 357, 2801, and 2802.

Researchers use cluster analysis to study protein shape and function. Each green circle represents one potential shape of the protein mitoNEET. The longer the blue line between two circles, the greater the differences between the shapes. Most shapes are similar; they fall into three clusters that are represented by the three images of the protein. From a Rice University news release. Graduate student Elizabeth Baxter and Patricia Jennings, professor of chemistry and biochemistry at UCSD, collaborated with José Onuchic, a physicist at Rice University, on this work.

NMR solution structure of a plant protein that may function in host defense. This protein was expressed in a convenient and efficient wheat germ cell-free system. Featured as the June 2007 Protein Structure Initiative Structure of the Month.

PETase enzyme degrades polyester plastic (polyethylene terephthalate, or PET) into monohydroxyethyl terephthalate (MHET). Then, MHETase enzyme degrades MHET into its constituents ethylene glycol (EG) and terephthalic acid (TPA).

Find these in the RCSB Protein Data Bank: PET hydrolase (PDB entry 5XH3) and MHETase (PDB entry 6QGA).

This image shows a cell in two stages of division: prometaphase (top) and metaphase (bottom). To form identical daughter cells, chromosome pairs (blue) separate via the attachment of microtubules made up of tubulin proteins (pink) to specialized structures on centromeres (green).

Gram-negative bacteria perform molecular acrobatics just to eat. Because they're encased by two membranes, they must haul nutrients across both. To test one theory of how the bacteria manage this feat, researchers used computer simulations of two proteins involved in importing vitamin B12. Here, the protein (red) anchored in the inner membrane of bacteria tugs on a much larger protein (green and blue) in the outer membrane. Part of the larger protein unwinds, creating a pore through which the vitamin can pass.

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.

Closeup of C. elegans, tiny roundworms, with a ribosomal protein glowing red and muscle fibers glowing green. Researchers used these worms to study a molecular pathway that affects aging. The ribosomal protein is involved in protein translation and may play a role in dietary restriction-induced longevity. Image created using confocal microscopy.
View single roundworm here 6581.
View group of roundworms here 6582.

This illustration shows, in simplified terms, how the CRISPR-Cas9 system can be used as a gene-editing tool.

For an explanation and overview of the CRISPR-Cas9 system, see the iBiology video, and download the four images of the CRIPSR illustration here.

A spore from the bacterium Bacillus subtilis shows four outer layers that protect the cell from harsh environmental conditions.

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.

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

For thousands of years, Chinese herbalists have treated malaria using Chang Shan, a root extract from a type of hydrangea that grows in Tibet and Nepal. Recent studies have suggested Chang Shan can also reduce scar formation, treat multiple sclerosis and even slow cancer progression.

Rhodopsin is a pigment in the rod cells of the retina (back of the eye). It is extremely light-sensitive, supporting vision in low-light conditions. Here, it is attached to arrestin, a protein that sends signals in the body. This structure was determined using an X-ray free electron laser.

A study using Caulobacter crescentus showed that some bacteria use just-in-time processing, much like that used in industrial delivery, to make the glue that allows them to attach to surfaces, an important step in the infection process for many disease-causing bacteria. In the image shown, this freshwater bacterium has a holdfast at the top and a propelling flagellum at the end. From an Indiana University news release.

An atomic force microscopy image shows DNA folded into an intricate, computer-designed structure. Image is featured on Biomedical Beat blog post Cool Image: DNA Origami. See also related image 3689 .

A drug's life in the body. Medicines taken by mouth (oral) pass through the liver before they are absorbed into the bloodstream. Other forms of drug administration bypass the liver, entering the blood directly. See 2527 for an unlabeled version of this illustration. Featured in Medicines By Design.

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.

A scanning electron microscope image of an activated mast cell. This image illustrates the interesting topography of the cell membrane, which is populated with receptors. The distribution of receptors may affect cell signaling. This image relates to a July 27, 2009 article in Computing Life.

A model of thymidylate synthase complementing protein from Thermotoga maritime.

Yeast cells with nuclear envelopes shown in magenta and tubulin shown in light blue. The nuclear envelope defines the borders of the nucleus, which houses DNA. Tubulin is a protein that makes up microtubules—strong, hollow fibers that provide structure to cells and help direct chromosomes during cell division. This image was captured using wide-field microscopy with deconvolution.

Related to images 6791, 6792, 6793, 6794, 6797, and videos 6795 and 6796.

The green in this image highlights a protein called TonB, which is produced by many gram-negative bacteria, including those that cause typhoid fever, meningitis and dysentery. TonB lets bacteria take up iron from the host's body, which they need to survive. More information about the research behind this image can be found in a Biomedical Beat Blog posting from August 2013.

Analysis of 68 million-year-old collagen molecule fragments preserved in a T. rex femur confirmed what paleontologists have said for decades: Dinosaurs are close relatives of chickens, ostriches, and to a lesser extent, alligators. A Harvard University research team, including NIGMS-supported postdoctoral research fellow Chris Organ, used sophisticated statistical and computational tools to compare the ancient protein to ones from 21 living species. Because evolutionary processes produce similarities across species, the methods and results may help illuminate other areas of the evolutionary tree. Featured in the May 21, 2008 Biomedical Beat.

This is a magnified view of an Arabidopsis thaliana leaf eight days after being infected with the pathogen Hyaloperonospora arabidopsidis, which is closely related to crop pathogens that cause 'downy mildew' diseases. It is also more distantly related to the agent that caused the Irish potato famine. The veins of the leaf are light blue; in darker blue are the pathogen's hyphae growing through the leaf. The small round blobs along the length of the hyphae are called haustoria; each is invading a single plant cell to suck nutrients from the cell. Jeff Dangl and other NIGMS-supported researchers investigate how this pathogen and other like it use virulence mechanisms to suppress host defense and help the pathogens grow.

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 (shown in red) have invaded the worm’s gut cells (the large blue dots are the cells' nuclei) 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 5778.

X-ray co-crystal structure of Src kinase bound to a DNA-templated macrocycle inhibitor. Related to 3413, 3415, 3416, 3417, 3418, and 3419.

Animation for the vesicular shuttle model of Golgi transport.

Shiga toxin (green) is sorted from the endosome into membrane tubules (red), which then pinch off and move to the Golgi apparatus.

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.

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.

Peripheral nerve cells made from human embryonic stem cell-derived neural crest stem cells. The nuclei are shown in blue, and nerve cell proteins peripherin and beta-tubulin (Tuj1) are shown in green and red, respectively. Related to image 3264. Image is featured in October 2015 Biomedical Beat blog post Cool Images: A Halloween-Inspired Cell Collection.

This video condenses 6.5 minutes into less than a minute to show how the toxin in bee venom, called melittin, destroys an animal or bacterial cell. What looks like a red balloon is an artificial cell filled with red dye. Melittin molecules are colored green and float on the cell's surface like twigs on a pond. As melittin accumulates on the cell's membrane, the membrane expands to accommodate it. In the video, the membrane stretches into a column on the left. When melittin levels reach a critical threshold, countless pinhole leaks burst open in the membrane. The cell's vital fluids (red dye in the video) leak out through these pores. Within minutes, the cell collapses. More information about the research behind this image can be found in a Biomedical Beat Blog posting from September 2013.

This image results from a research project to visualize which regions of the adult fruit fly (Drosophila) brain derive from each neural stem cell. First, researchers collected several thousand fruit fly larvae and fluorescently stained a random stem cell in the brain of each. The idea was to create a population of larvae in which each of the 100 or so neural stem cells was labeled at least once. When the larvae grew to adults, the researchers examined the flies’ brains using confocal microscopy.
With this technique, the part of a fly’s brain that derived from a single, labeled stem cell “lights up.” The scientists photographed each brain and digitally colorized its lit-up area. By combining thousands of such photos, they created a three-dimensional, color-coded map that shows which part of the Drosophila brain comes from each of its ~100 neural stem cells. In other words, each colored region shows which neurons are the progeny or “clones” of a single stem cell. This work established a hierarchical structure as well as nomenclature for the neurons in the Drosophila brain. Further research will relate functions to structures of the brain.

Related to image 5838 and video 5843.

A light organ (~0.5 mm across) of a Hawaiian bobtail squid, Euprymna scolopes, stained blue. At the time of this image, the crypts within the tissues of only one side of the organ had been colonized by green-fluorescent protein-labeled Vibrio fischeri cells, which can be seen here in green. This image was taken using confocal fluorescence microscopy.

Related to images 7016, 7017, 7018, and 7019.

These neurons are derived from mouse embryonic stem cells. Red shows cells making a protein called TH that is characteristic of the neurons that degenerate in Parkinson's disease. Green indicates a protein that's found in all neurons. Blue indicates the nuclei of all cells. Studying dopaminergic neurons can help researchers understand the origins of Parkinson's disease and could be used to screen potential new drugs. Image and caption information courtesy of the California Institute for Regenerative Medicine. Related to images 3270 and 3285.

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 3793.