CCD-1 is an enzyme produced by the bacterium Clostridioides difficile that helps it resist antibiotics. Using X-ray crystallography, researchers determined the structure of a complex between CCD-1 and the antibiotic cefotaxime (purple, yellow, and blue molecule). The structure revealed that CCD-1 provides extensive hydrogen bonding (shown as dotted lines) and stabilization of the antibiotic in the active site, leading to efficient degradation of the antibiotic.

Related to images 6764, 6765, and 6766.

This fingertip-shaped group of lights is a microscopic crystal called a quantum dot. About 10,000 times thinner than a sheet of paper, the dot radiates brilliant colors under ultraviolet light. Dots such as this one allow researchers to label and track individual molecules in living cells and may be used for speedy disease diagnosis, DNA testing, and screening for illegal drugs.

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

Yeast cells with nuclei shown in green and contractile rings shown in magenta. Nuclei store DNA, and contractile rings help cells divide. This image was captured using wide-field microscopy with deconvolution.

Related to images 6791, 6793, 6794, 6797, 6798, and videos 6795 and 6796.

Multicellular yeast called snowflake yeast that researchers created through many generations of directed evolution from unicellular yeast. Cells are connected to one another by their cell walls, shown in blue. Stained cytoplasm (green) and membranes (magenta) show that the individual cells remain separate. This image was captured using spinning disk confocal microscopy.

Related to images 6969 and 6971.

This image shows how the CRISPR surveillance complex is disabled by two copies of anti-CRISPR protein AcrF1 (red) and one AcrF2 (light green). These anti-CRISPRs block access to the CRISPR RNA (green tube) preventing the surveillance complex from scanning and targeting invading viral DNA for destruction.

Duplicated pair of chromosomes have exchanged material.

A fruit fly (Drosophila melanogaster) egg chamber with microtubules shown in green and actin filaments shown in red. Egg chambers are multicellular structures in fruit flies ovaries that each give rise to a single egg. Microtubules and actin filaments give the chambers structure and shape. This image was captured using a confocal microscope.

More information on the research that produced this image can be found in the Current Biology paper "Gatekeeper function for Short stop at the ring canals of the Drosophila ovary" by Lu et al.

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.

Ovarioles in female insects are tubes in which egg cells (called oocytes) form at one end and complete their development as they reach the other end of the tube. This image, taken with a confocal microscope, shows ovarioles in a very popular lab animal, the fruit fly Drosophila. The basic structure of ovarioles supports very rapid egg production, with some insects (like termites) producing several thousand eggs per day. Each insect ovary typically contains four to eight ovarioles, but this number varies widely depending on the insect species.

Scientists use insect ovarioles, for example, to study the basic processes that help various insects, including those that cause disease (like some mosquitos and biting flies), reproduce very quickly.

The image visualizes a part of the yeast molecular interaction network. The lines in the network represent connections among genes (shown as little dots) and different-colored networks indicate subnetworks, for instance, those in specific locations or pathways in the cell. Researchers use gene or protein expression data to build these networks; the network shown here was visualized with a program called Cytoscape. By following changes in the architectures of these networks in response to altered environmental conditions, scientists can home in on those genes that become central "hubs" (highly connected genes), for example, when a cell encounters stress. They can then further investigate the precise role of these genes to uncover how a cell's molecular machinery deals with stress or other factors. Related to images 3732 and 3733.

Bioengineers were able to coax bacteria to blink in unison on microfluidic chips. This image shows a small chip with about 500 blinking bacterial colonies or biopixels. Related to images 3265 and 3268. From a UC San Diego news release, "Researchers create living 'neon signs' composed of millions of glowing bacteria."

This illustration of an epoxide-opening cascade promoted by water emulates the proposed biosynthesis of some of the Red Tide toxins.

A model of the molecule himastatin overlaid on an image of Bacillus subtilis bacteria. Scientists first isolated himastatin from the bacterium Streptomyces himastatinicus, and the molecule shows antibiotic activity. The researchers who created this image developed a new, more concise way to synthesize himastatin so it can be studied more easily. They also tested the effects of himastatin and derivatives of the molecule on B. subtilis.

More information about the research that produced this image can be found in the Science paper “Total synthesis of himastatin” by D’Angelo et al.

Related to image 6848 and video 6851.

Each point in these colorful patchworks represents the correlation between two sleep-associated genes in fruit flies. Vibrant reds and oranges represent high and intermediate degrees of association between the genes, respectively. Genes in these areas show similar activity patterns in different fly lines. Cool blues represent gene pairs where one partner's activity is high and the other's is low. The green areas show pairs with activities that are not correlated. These quilt-like depictions help illustrate a recent finding that genes act in teams to influence sleep patterns.

These ripples of color represent the outer membrane of the nucleus inside an astrocyte, a star-shaped cell inside the brain. Some proteins (green) act as keys to unlock other proteins (red) that form gates to let small molecules in and out of the nucleus (blue). Visualizing these different cell components at the boundary of the astrocyte nucleus enables researchers to study the molecular and physiological basis of neurological disorders, such as hydrocephalus, a condition in which too much fluid accumulates in the brain, and scar formation in brain tissue leading to abnormal neuronal activity affecting learning and memory. Scientists have now identified a pathway may be common to many of these brain diseases and begun to further examine it to find ways to treat certain brain diseases and injuries.

On the left, a cross-section slice of a rat pancreas cell captured using cryo-electron tomography (cryo-ET). On the right, a 3D, color-coded version of the image highlighting cell structures. Visible features include microtubules (neon-green rods), ribosomes (small yellow circles), and vesicles (dark-blue circles). These features are surrounded by the partially visible endoplasmic reticulum (light blue). The black line at the bottom right of the left image represents 200 nm. Related to image 6607.

To become products, reactants must overcome an energy hill. See image 2525 for an unlabeled version of this illustration. Featured in The Chemistry of Health.

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.

Sepsis is the body’s overactive and extreme response to an infection. More than 1.7 million people get sepsis each year in the United States. Without prompt treatment, sepsis can lead to tissue damage, organ failure, and death. Many NIGMS-supported researchers are working to improve sepsis diagnosis and treatment. Learn more with our sepsis featured topic page.

See 6551 for the Spanish version of this infographic.

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.

The world's smallest motor, ATP synthase, generates energy for the cell. See image 2517 for an unlabeled version of this illustration. Featured in The Chemistry of Health.

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.

A representation of a patient’s brain waves after receiving the anesthetic propofol. All anesthetics create brain wave changes that vary depending on the patient’s age and the type and dose of anesthetic used. These changes are visible in raw electroencephalogram (EEG) readings, but they’re easier to interpret using a spectrogram where the signals are broken down by time (x-axis), frequency (y-axis), and power (color scale). This spectrogram shows the changes in brain waves before, during, and after propofol-induced anesthesia. The patient is unconscious from minute 5, upon propofol administration, through minute 69 (change in power and frequency). But, between minutes 35 and 48, the patient fell into a profound state of unconsciousness (disappearance of dark red oscillations between 8 to 12 Hz), which required the anesthesiologist to adjust the rate of propofol administration. The propofol was stopped at minute 62 and the patient woke up around minute 69.

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.

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.

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.

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.

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 absent in the filopodi-like structures based leading edge of ARPC3-/- fibroblasts cells. Related to images 3328, 3330, 3331, 3332, and 3333.

Kinases are enzymes that add phosphate groups (red-yellow structures) to proteins (green), assigning the proteins a code. In this reaction, an intermediate molecule called ATP (adenosine triphosphate) donates a phosphate group from itself, becoming ADP (adenosine diphosphate). See image 2534 for an unlabeled version of this illustration. Featured in Medicines By Design.

This structure from an amyloid-forming prion protein shows one way beta sheets can stack. Image originally appeared in a December 2012 PLOS Biology paper.

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 research organism Arabidopsis thaliana forms a large molecular machine called a resistosome to fight off infections. This illustration shows the top and side views of the fully-formed resistosome assembly (PDB entry 6J5T), composed of different proteins including one the plant uses as a decoy, PBL2 (dark blue), that gets uridylylated to begin the process of building the resistosome (uridylyl groups in magenta). Other proteins include RSK1 (turquoise) and ZAR1 (green) subunits. The ends of the ZAR1 subunits (yellow) form a funnel-like protrusion on one side of the assembly (seen in the side view). The funnel can carry out the critical protective function of the resistosome by inserting itself into the cell membrane to form a pore, which leads to a localized programmed cell death. The death of the infected cell helps protect the rest of the plant.

What looks like a Native American dream catcher is really a network of social interactions within a community. The red dots along the inner and outer circles represent people, while the different colored lines represent direct contact between them. All connections originate from four individuals near the center of the graph. Modeling social networks can help researchers understand how diseases spread.

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

Staphylococcus aureus bacteria (blue) on the porous coating of a femoral hip stem used in hip replacement surgery. The relatively rough surface of an implant is a favorable environment for bacteria to attach and grow. This can lead to the development of biofilms, which can cause infections. The researchers who took this image are working to understand where biofilms are likely to develop. This knowledge could support the prevention and treatment of infections. A scanning electron microscope was used to capture this image.

More information on the research that produced this image can be found in the Antibiotics paper "Free-floating aggregate and single-cell-initiated biofilms of Staphylococcus aureus" by Gupta et al.

Related to image 6803 and video 6805.

Kinases are enzymes that add phosphate groups (red-yellow structures) to proteins (green), assigning the proteins a code. In this reaction, an intermediate molecule called ATP (adenosine triphosphate) donates a phosphate group from itself, becoming ADP (adenosine diphosphate). See image 2535 for a labeled version of this illustration. Featured in Medicines By Design.

A model of a Geobacter sulfurreducens nanowire created from cryo-electron microscopy images. The bacterium conducts electricity through these nanowires, which are made up of protein and iron-containing molecules.

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 illustration shows a protein substrate (red) that is bound through its ubiquitin chain (blue) to one of the ubiquitin receptors of the proteasome (Rpn10, yellow). The substrate's flexible engagement region 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 small 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 video 3764.

Time lapse series shows short dynamin assemblies (not visible) constricting a lipid tube to make a "beads on a string" appearance, then cutting off one of the beads i.e., catalyzing membrane fission). The lipids are fluorescent (artificially colored). Ramachandran R, Pucadyil T.J., Liu Y.W., Acharya S., Leonard M., Lukiyanchuk V., Schmid S.L. 2009. Membrane insertion of the pleckstrin homology domain variable loop 1 is critical for dynamin-catalyzed vesicle scission. Mol Biol Cell. 2009 20:4630-9.

Related to image 5871.

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.

In this video, Rice University scientists used molecular modeling with a mathematical algorithm called AWSEM (for associative memory, water-mediated, structure and energy model) and structural data to analyze how a transcription factor called nuclear factor kappa B (NFkB) is removed from DNA to stop gene activation. AWSEM uses the interacting energies of their components to predict how proteins fold. At the start, the NFkB dimer (green and yellow, in the center) grips DNA (red, to the left), which activates the transcription of genes. IkB (blue, to the right), an inhibitor protein, stops transcription when it binds to NFkB and forces the dimer to twist and release its hold on DNA. The yellow domain at the bottom of IkB is the PEST domain, which binds first to NFkB. For more details about this mechanism called molecular stripping, see here.

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. Related to image 3586.
For more information about relapsing fever, see https://www.cdc.gov/relapsing-fever/index.html.
This image is part of the Life: Magnified collection, which was displayed in the Gateway Gallery at Washington Dulles International Airport June 3, 2014, to January 21, 2015.

Merged fluorescent images of symmetrically (left) or asymmetrically (right) elongating HeLa cells at the end of early anaphase (magenta) and late anaphase (green). Chromosomes and cortical actin are visualized by expressing mCherry-histone H2B and Lifeact-mCherry. Scale bar, 10µm. See the PubMed abstract of this research.

Early on, this Arabidopsis plant embryo picks sides: While one end will form the shoot, the other will take root underground. Short pieces of RNA in the bottom half (blue) make sure that shoot-forming genes are expressed only in the embryo's top half (green), eventually allowing a seedling to emerge with stems and leaves. Like animals, plants follow a carefully orchestrated polarization plan and errors can lead to major developmental defects, such as shoots above and below ground. Because the complex gene networks that coordinate this development in plants and animals share important similarities, studying polarity in Arabidopsis--a model organism--could also help us better understand human development.

Cell-like compartments spontaneously emerge from scrambled frog eggs, with nuclei (blue) from frog sperm. Endoplasmic reticulum (red) and microtubules (green) are also visible. Regions without nuclei formed smaller compartments. Video created using epifluorescence microscopy.

For more photos of cell-like compartments from frog eggs view: 6584, 6585, 6586, 6591, 6592, and 6593.

For videos of cell-like compartments from frog eggs view: 6587, 6589, and 6590.

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.

Under the microscope, an E. coli cell lights up like a fireball. Each bright dot marks a surface protein that tells the bacteria to move toward or away from nearby food and toxins. Using a new imaging technique, researchers can map the proteins one at a time and combine them into a single image. This lets them study patterns within and among protein clusters in bacterial cells, which don't have nuclei or organelles like plant and animal cells. Seeing how the proteins arrange themselves should help researchers better understand how cell signaling works.

Lab-made liposomes contract where Z rings have gathered together and the constriction forces are greatest (arrows). The top picture shows a liposome, and the bottom picture shows fluorescence from Z rings (arrows) inside the same liposome simultaneously.