Homology-based loop modeling yields more complete crystallographic protein structures
Abstract
Inherent protein flexibility, poor or low-resolution diffraction data or poorly defined electron-density maps often inhibit the building of complete structural models during X-ray structure determination. However, recent advances in crystallographic refinement and model building often allow completion of previously missing parts. This paper presents algorithms that identify regions missing in a certain model but present in homologous structures...
Paper Details
Title
Homology-based loop modeling yields more complete crystallographic protein structures
Published Date
Aug 8, 2018
Journal
Volume
5
Issue
5
Pages
585 - 594
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Notes
History