Results 61 to 70 of about 6,313,615 (343)

Structural and biochemical analysis of a B12 superbinder

FEBS Letters, EarlyView.
BtuG proteins are vitamin B12 scavengers in Bacteroides thetaiotaomicron, a dominant human gut bacterium. We present crystal structures of three BtuG homologs bound to cobalamin and its precursor cobinamide, revealing picomolar binding affinities, among the highest known for any natural protein.
Jose M. Martinez Felices, Jacob J. Whittaker, Dirk J. Slotboom, Albert Guskov   +3 more
wiley   +1 more source

C-SPAM: an open-source time-resolved specimen vitrification device with light-activated molecules

IUCrJ
Molecular structures can be determined in vitro and in situ with cryo-electron microscopy (cryo-EM). Specimen preparation is a major obstacle in cryo-EM. Typical sample preparation is orders of magnitude slower than biological processes.
Alejandra Montaño Romero, Calli Bonin, Edward C. Twomey   +2 more
doaj   +1 more source

Diverse Morphology and Structural Features of Old and New World Hantaviruses

Viruses, 2019
To further understanding of the structure and morphology of the Orthohantavirus, family Hantaviridae, we have employed cryo-electron microscopy (cryo-EM) for three New World hantaviruses: Andes (ANDV), Sin Nombre (SNV), and Black Creek Canal (BCCV ...
Amar Parvate, Evan P. Williams, Mariah K. Taylor, Yong-Kyu Chu, Jason Lanman, Erica Ollmann Saphire, Colleen B. Jonsson   +6 more
doaj   +1 more source

Cryo-EM strikes gold [PDF]

Nature Methods, 2015
Gold supports nearly eliminate unwanted specimen motion in cryo-electron microscopy, enabling high-resolution structure determination of challenging proteins.
openaire   +2 more sources

Cryo-EM structure of the exocyst complex [PDF]

Nature Structural & Molecular Biology, 2018
The exocyst is an evolutionarily conserved octameric protein complex that mediates the tethering of post-Golgi secretory vesicles to the plasma membrane during exocytosis and is implicated in many cellular processes such as cell polarization, cytokinesis, ciliogenesis and tumor invasion. Using cryo-EM and chemical cross-linking MS (CXMS), we solved the
Kunrong Mei, Yan Li, Shaoxiao Wang, Guangcan Shao, Jia Wang, Yuehe Ding, Guangzuo Luo, Peng Yue, Jun-Jie Liu, Xinquan Wang, Meng-Qiu Dong, Hong-Wei Wang, Wei Guo   +12 more
openaire   +2 more sources

Structures of mycobacterial 3‐methylcrotonyl‐CoA carboxylase reveal carrier‐domain translocation between catalytic sites

FEBS Letters, EarlyView.
Mycobacterial 3‐methylcrotonyl‐CoA carboxylase uses a mobile biotin‐carrying domain to shuttle a carboxyl group between two catalytic sites, enabling carboxylation of 3‐methylcrotonyl‐CoA during leucine breakdown. Cryo‐electron microscopy captures the carrier at both sites and reveals an inward loop movement that may prevent futile rebinding to the ...
Ajit Yadav, Bogdan I. Florea, Sebastian Geibel   +2 more
wiley   +1 more source

Cryo-EM of nucleosome core particle interactions in trans

Scientific Reports, 2018
Nucleosomes, the basic unit of chromatin, are repetitively spaced along DNA and regulate genome expression and maintenance. The long linear chromatin molecule is extensively condensed to fit DNA inside the nucleus.
Silvija Bilokapic, Mike Strauss, Mario Halic   +2 more
doaj   +1 more source

Low cost, high performance processing of single particle cryo-electron microscopy data in the cloud

eLife, 2015
The advent of a new generation of electron microscopes and direct electron detectors has realized the potential of single particle cryo-electron microscopy (cryo-EM) as a technique to generate high-resolution structures.
Michael A Cianfrocco, Andres E Leschziner   +1 more
doaj   +1 more source

The Current Revolution in Cryo-EM [PDF]

Biophysical Journal, 2016
Structural biology is the study of the molecular architecture of proteins and nucleic acids, which are the basis for all life forms. Structural biology came into its own as a field during the 1950s when the atomic structures of DNA (1) and several globular proteins (2) were solved.
openaire   +2 more sources

The heterodimeric amino acid transporters (HAT) of the SLC7/SLC3 family: A structure−function relationships and relevance to human pathology

FEBS Letters, EarlyView.
Heterodimeric amino acid transporters consist of SLC7 and SLC3 family proteins arranged in a conserved structural organization. They regulate nutrient transport across cell membranes, supporting essential cellular functions. These transporters also contribute to xenobiotic/drug uptake and distribution.
Mariafrancesca Scalise, Tiziano Mazza, Raffaella Scanga, Lara Console, Michele Galluccio, Cesare Indiveri   +5 more
wiley   +1 more source