Get 20M+ Full-Text Papers For Less Than $1.50/day. Start a 14-Day Trial for You or Your Team.

Learn More →

Direct Methods in Protein Electron Crystallography: the Ab Initio Structure Determination of Two Membrane Protein Structures in Projection using Maximum Entropy and Likelihood

Direct Methods in Protein Electron Crystallography: the Ab Initio Structure Determination of Two... Using maximum entropy and likelihood, an ab initio phase determination was carried out in projection at ca 6-10 A resolution for two dissimilar membrane proteins: the Omp F porin from the outer membrane of E. coli (largely -sheet) and halorhodopsin (largely -helix). Accurate phase information found for the most likely solutions enabled potential maps to be calculated that contained most of the essential structural details of these macromolecules without the need for any image, derived phases as a starting set for phase extension or the necessity to use envelopes or electron-density histograms. A comparison with earlier calculations using the Sayre-Hughes equation coupled with phase annealing and the Luzzati flatness criterion used as a figure of merit is made. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Acta Crystallographica Section A Foundations of Crystallography International Union of Crystallography

Direct Methods in Protein Electron Crystallography: the Ab Initio Structure Determination of Two Membrane Protein Structures in Projection using Maximum Entropy and Likelihood

Direct Methods in Protein Electron Crystallography: the Ab Initio Structure Determination of Two Membrane Protein Structures in Projection using Maximum Entropy and Likelihood


Abstract

Using maximum entropy and likelihood, an ab initio phase determination was carried out in projection at ca 6-10 A resolution for two dissimilar membrane proteins: the Omp F porin from the outer membrane of E. coli (largely -sheet) and halorhodopsin (largely -helix). Accurate phase information found for the most likely solutions enabled potential maps to be calculated that contained most of the essential structural details of these macromolecules without the need for any image, derived phases as a starting set for phase extension or the necessity to use envelopes or electron-density histograms. A comparison with earlier calculations using the Sayre-Hughes equation coupled with phase annealing and the Luzzati flatness criterion used as a figure of merit is made.

Loading next page...
 
/lp/international-union-of-crystallography/direct-methods-in-protein-electron-crystallography-the-ab-initio-n2DsySUwRO

References (6)

Publisher
International Union of Crystallography
Copyright
Copyright (c) 1996 International Union of Crystallography
ISSN
0108-7673
eISSN
1600-5724
DOI
10.1107/S0108767396008744
Publisher site
See Article on Publisher Site

Abstract

Using maximum entropy and likelihood, an ab initio phase determination was carried out in projection at ca 6-10 A resolution for two dissimilar membrane proteins: the Omp F porin from the outer membrane of E. coli (largely -sheet) and halorhodopsin (largely -helix). Accurate phase information found for the most likely solutions enabled potential maps to be calculated that contained most of the essential structural details of these macromolecules without the need for any image, derived phases as a starting set for phase extension or the necessity to use envelopes or electron-density histograms. A comparison with earlier calculations using the Sayre-Hughes equation coupled with phase annealing and the Luzzati flatness criterion used as a figure of merit is made.

Journal

Acta Crystallographica Section A Foundations of CrystallographyInternational Union of Crystallography

Published: Nov 1, 1996

There are no references for this article.