1ejg
From Proteopedia
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(New page: 200px<br /><applet load="1ejg" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ejg, resolution 0.54Å" /> '''CRAMBIN AT ULTRA-HIG...)
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Revision as of 11:56, 20 November 2007
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CRAMBIN AT ULTRA-HIGH RESOLUTION: VALENCE ELECTRON DENSITY.
Overview
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.
About this Structure
1EJG is a Single protein structure of sequence from Crambe hispanica subsp. abyssinica. Full crystallographic information is available from OCA.
Reference
Accurate protein crystallography at ultra-high resolution: valence electron distribution in crambin., Jelsch C, Teeter MM, Lamzin V, Pichon-Pesme V, Blessing RH, Lecomte C, Proc Natl Acad Sci U S A. 2000 Mar 28;97(7):3171-6. PMID:10737790
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