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

Crystals of porcine alpha amylase protein created for X-ray crystallography, which can reveal detailed, three-dimensional protein structures.

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.

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.

RNA polymerase (purple) is a complex enzyme at the heart of transcription. During this process, the enzyme unwinds the DNA double helix and uses one strand (darker orange) as a template to create the single-stranded messenger RNA (green), later used by ribosomes for protein synthesis.

From the RNA polymerase II elongation complex of Saccharomyces cerevisiae (PDB entry 1I6H) as seen in PDB-101's What is a Protein? video.

An RNA molecule dynamically refolds itself as it is being synthesized. When the RNA is short, it ties itself into a “knot” (dark purple). For this domain to slip its knot, about 5 seconds into the video, another newly forming region (fuchsia) wiggles down to gain a “toehold.” About 9 seconds in, the temporarily knotted domain untangles and unwinds. Finally, at about 23 seconds, the strand starts to be reconfigured into the shape it needs to do its job in the cell.

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.

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

CellPack image of the H1N1 influenza virus, with hemagglutinin and neuraminidase glycoproteins in green and red, respectively, on the outer envelope (white); matrix protein in gray, and ribonucleoprotein particles inside the virus in red and green. Related to image 6356.

Just as our bodies rely on bones for structural support, our cells rely on a cellular skeleton. In addition to helping cells keep their shape, this cytoskeleton transports material within cells and coordinates cell division. One component of the cytoskeleton is a protein called tubulin, shown here as thin strands.

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

The lubber grasshopper, found throughout the southern United States, is frequently used in biology classes to teach students about the respiratory system of insects. Unlike mammals, which have red blood cells that carry oxygen throughout the body, insects have breathing tubes that carry air through their exoskeleton directly to where it's needed. This image shows the breathing tubes embedded in the weblike sheath cells that cover developing egg chambers.

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

Model of the enzyme aminopeptidase N from the human pathogen Neisseria meningitidis, which can cause meningitis epidemics. The structure provides insight on the active site of this important molecule.

The G switch allows our bodies to respond rapidly to hormones. See images 2537 and 2538 for labeled versions of this image. Featured in Medicines By Design.

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.

Force vectors computed from actin cytoskeleton flow. This is an example of NIH-supported research on single-cell analysis. Related to 2798, 2800, 2801, 2802 and 2803.

Cytoplasmic linker protein (CLIP)-170 is a microtubule plus-end-tracking protein that regulates microtubule dynamics and links microtubule ends to different intracellular structures. In this movie, the gene for CLIP-170 has been fused with green fluorescent protein (GFP). When the protein is expressed in cells, the activities can be monitored in real time. Here, you can see CLIP-170 streaming towards the edges of the cell.

This illustration represents the early life of a protein—specifically, apomyoglobin—as it is synthesized by a ribosome and emerges from the ribosomal tunnel, which contains the newly formed protein's conformation. The synthesis occurs in the complex swirl of the cell medium, filled with interactions among many molecules. Researchers in Silvia Cavagnero's laboratory are studying the structure and dynamics of newly made proteins and polypeptides using spectroscopic and biochemical techniques.

The receptor is shown bound to an antagonist, eticlopride