Results 11 to 20 of about 6,313,615 (343)
Cryo-EM data collection, refinement, and validation statistics.
, 2023 Cryo-EM data collection, refinement, and validation statistics.
Kai Virumäe (15148137) +29 more
core +7 more sources
Cryo-EM data collection and refinement statistics.
, 2023 Cryo-EM data collection and refinement statistics.
Shasha Zhou (5590880) +18 more
core +4 more sources
Comparative assessment of crystallographic and cryo-EM models in the Protein Data Bank. [PDF]
FEBS Open BioRaw data obtained by X‐ray crystallography or cryo‐EM result in experimental maps, ultimately fitted by atomic models. Although the physical principles are different, the final results can be viewed, compared, and evaluated in the same way. With cryogenic electron microscopy (cryo‐EM) on track to surpass X‐ray crystallography as the preferred method ...
Wlodawer A +7 more
europepmc +2 more sources
Cryo‐EM for Small Molecules [PDF]
Current Protocols, 2022 AbstractIn recent years, protein structure analysis using cryo‐electron microscopy(cryo‐EM) has expanded and improved. In this review, we discuss many recent improvements to the field, the problems those improvements hope to solve, and some of the still unanswered questions.
Cabral, Angela +2 more
openaire +3 more sources
Bsoft: Image Processing for Structural Biology
Bio-Protocol, 2022 Bsoft is a software package primarily developed for processing electron micrographs, with the goal of determining the structures of biologically relevant molecules, molecular assemblies, and parts of cells. However, it incorporates many ways to deal with
Bernard Heymann
doaj +1 more source
IUCrJ, 2022 The 2022 meeting of the American Crystallographic Association in Portland was an inspiring event, addressing a range of both conventional and emerging themes in structural biology. The increasing emphasis at the conference on methods outside the conventional envelope of crystallography, especially cryo-electron microscopy, is discussed.
Sriram Subramaniam +2 more
openaire +4 more sources
Cryo-EM structural determination of PfFNT–MMV007839.
, 2021 (A) A representative cryo-EM micrograph of PfFNT- MMV007839. (B) A representative 2D classification average. (C) Flowchart for EM data processing of datasets. Details can be found in the Methods. cryo-EM, cryo-electron microscopy; EM, electron microscopy;
Yanxia Zhou (1447465) +17 more
core +1 more source
Bayesian cryo-EM Refinement [PDF]
Biophysical Journal, 2015 In light of recent high-resolution cryo-electron-microscopy (cryo-EM) structures of large complexes, modeling atom coordinates into cryo-EM densities faces new challenges. Though high-resolution structures provide more data, finding the best-fitting structure with current refinement methods is more difficult with increased resolution, because the used ...
Blau, Christian +4 more
openaire +3 more sources
Cryo-ET and cryo-EM data collection and processing parameters.
, 2023 Cryo-ET and cryo-EM data collection and processing parameters.
Achilleas S. Frangakis (107667) +4 more
core +1 more source
Cryo-EM structural determination of PfFNT.
, 2021 (A) A representative cryo-EM micrograph of PfFNT. (B) A representative 2D classification average. (C) Flowchart for EM data processing of PfFNT datasets. Details can be found in the Methods. cryo-EM, cryogenic-electron microscopy; EM, electron microscopy;
Yanxia Zhou (1447465) +17 more
core +1 more source