TY - JOUR
T1 - Fitting of high-resolution structures into electron microscopy reconstruction images
AU - Fabiola, Felcy
AU - Chapman, Michael S.
N1 - Funding Information:
We gratefully acknowledge the contributions of colleagues, Jinghua Tang, Eric Blanc, Zhi Chen, and, particularly, Andrei Korostelev, to earlier versions of the programs and of our EM collaborators Lifan Chen, Jun Liu, Ken Taylor, Hiaxao Gao, and Joachim Frank. Software is distributed under license at no cost to academic institutions. Details and license agreements are available at http://www.sb.fsu.edu/~chapman . This work was supported in part by the National Institutes of Health P01 GM64676 (Timothy A. Cross) subproject (M.S.C.).
PY - 2005/3
Y1 - 2005/3
N2 - Dynamic macromolecular assemblies, such as ribosomes, viruses, and muscle protein complexes, are often more amenable to visualization by electron microscopy than by high-resolution X-ray crystallography or NMR. When high-resolution structures of component structures are available, it is possible to build an atomic model that gives information about the molecular interactions at greater detail than the experimental resolution, due to constraints of modeling placed upon the interpretation. There are now several competing computational methods to search systematically for orientations and positions of components that match the experimental image density, and continuing developments will be reviewed. Attention is now also moving toward the related task of optimization, with flexible and/or multifragment models and sometimes with stereochemically restrained refinement methods. This paper will review the various approaches and describe advances in the authors' methods and applications of real-space refinement.
AB - Dynamic macromolecular assemblies, such as ribosomes, viruses, and muscle protein complexes, are often more amenable to visualization by electron microscopy than by high-resolution X-ray crystallography or NMR. When high-resolution structures of component structures are available, it is possible to build an atomic model that gives information about the molecular interactions at greater detail than the experimental resolution, due to constraints of modeling placed upon the interpretation. There are now several competing computational methods to search systematically for orientations and positions of components that match the experimental image density, and continuing developments will be reviewed. Attention is now also moving toward the related task of optimization, with flexible and/or multifragment models and sometimes with stereochemically restrained refinement methods. This paper will review the various approaches and describe advances in the authors' methods and applications of real-space refinement.
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U2 - 10.1016/j.str.2005.01.007
DO - 10.1016/j.str.2005.01.007
M3 - Article
C2 - 15766540
AN - SCOPUS:14844311200
SN - 0969-2126
VL - 13
SP - 389
EP - 400
JO - Structure
JF - Structure
IS - 3
ER -