1EJG: Crambin at Ultra-high Resolution: Valence Electron Density

Citation:
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.
PDB ID: 1EJGDownload
MMDB ID: 117754
PDB Deposition Date: 2000/3/2
Updated in MMDB: 2014/02 
Experimental Method:
x-ray diffraction
Resolution: 0.54  Å
Source Organism:
Similar Structures:
Biological Unit for 1EJG: monomeric; determined by author
Molecular Components in 1EJG
Label Count Molecule
Protein (1 molecule)
1
Crambin (Pro22,ser22/leu25,ile25)
Molecule annotation
* Click molecule labels to explore molecular sequence information.

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