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.
journal_name
Proc Natl Acad Sci U S Aauthors
Jelsch C,Teeter MM,Lamzin V,Pichon-Pesme V,Blessing RH,Lecomte Cdoi
10.1073/pnas.97.7.3171keywords:
subject
Has Abstractpub_date
2000-03-28 00:00:00pages
3171-6issue
7eissn
0027-8424issn
1091-6490pii
97/7/3171journal_volume
97pub_type
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