Fitting atomic models into electron‐microscopy maps

Fitting atomic models into electron‐microscopy maps Combining X‐ray crystallographically determined atomic structures of component domains or subunits with cryo‐electron microscopic three‐dimensional images at around 22 Å resolution can produce structural information that is accurate to about 2.2 Å resolution. In an initial step, it is necessary to determine accurately the absolute scale and absolute hand of the cryo‐electron microscopy map, the former of which can be off by up to 5%. It is also necessary to determine the relative height of density by using a suitable scaling function. Difference maps can identify, for instance, sites of glycosylation, the position of which helps to fit the component structures into the EM density maps. Examples are given from the analysis of alphaviruses, rhinovirus–receptor interactions and poliovirus–receptor interactions. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Acta Crystallographica Section D Wiley

Fitting atomic models into electron‐microscopy maps

Acta Crystallographica Section D, Volume 56 (10) – Oct 1, 2000

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Publisher
Wiley
Copyright
Copyright © 2000 Wiley Subscription Services, Inc., A Wiley Company
ISSN
1399-0047
eISSN
1399-0047
DOI
10.1107/S0907444900009562
Publisher site
See Article on Publisher Site

Abstract

Combining X‐ray crystallographically determined atomic structures of component domains or subunits with cryo‐electron microscopic three‐dimensional images at around 22 Å resolution can produce structural information that is accurate to about 2.2 Å resolution. In an initial step, it is necessary to determine accurately the absolute scale and absolute hand of the cryo‐electron microscopy map, the former of which can be off by up to 5%. It is also necessary to determine the relative height of density by using a suitable scaling function. Difference maps can identify, for instance, sites of glycosylation, the position of which helps to fit the component structures into the EM density maps. Examples are given from the analysis of alphaviruses, rhinovirus–receptor interactions and poliovirus–receptor interactions.

Journal

Acta Crystallographica Section DWiley

Published: Oct 1, 2000

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