Accurate protein crystallography at ultra-high resolution: valence electron distribution in crambin.

Abstract:

:The charge density distribution of a protein has been refined experimentally. Diffraction data for a crambin crystal were measured to ultra-high resolution (0.54 A) at low temperature by using short-wavelength synchrotron radiation. The crystal structure was refined with a model for charged, nonspherical, multipolar atoms to accurately describe the molecular electron density distribution. The refined parameters agree within 25% with our transferable electron density library derived from accurate single crystal diffraction analyses of several amino acids and small peptides. The resulting electron density maps of redistributed valence electrons (deformation maps) compare quantitatively well with a high-level quantum mechanical calculation performed on a monopeptide. This study provides validation for experimentally derived parameters and a window into charge density analysis of biological macromolecules.

authors

Jelsch C,Teeter MM,Lamzin V,Pichon-Pesme V,Blessing RH,Lecomte C

doi

10.1073/pnas.97.7.3171

keywords:

subject

Has Abstract

pub_date

2000-03-28 00:00:00

pages

3171-6

issue

7

eissn

0027-8424

issn

1091-6490

pii

97/7/3171

journal_volume

97

pub_type

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