1ejg | pdb_00001ejg

CRAMBIN AT ULTRA-HIGH RESOLUTION: VALENCE ELECTRON DENSITY.

spinqualitylabelsall models 1ejg, resolution 0.54Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1ejg is a 1 chain structure with sequence from Crambe hispanica subsp. abyssinica. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 1cbn, 1crn, 1ab1, 1cnr Resources: FirstGlance, OCA, RCSB, PDBsum Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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