1EJG

CRAMBIN AT ULTRA-HIGH RESOLUTION: VALENCE ELECTRON DENSITY.

Summary for 1EJG

• Entry DOI: 10.2210/pdb1ejg/pdb
• Related: 1AB1 1CBN 1CNR 1CRN
• Descriptor: CRAMBIN (PRO22,SER22/LEU25,ILE25) (1 entity in total)
• Functional Keywords: valence electron density, multi-substate, multipole refinement, plant protein
• Biological source: Crambe hispanica subsp. abyssinica
• Cellular location: Secreted: P01542
• Total number of polymer chains: 1
• Total formula weight: 4738.45

Authors

Jelsch, C.,Teeter, M.M.,Lamzin, V.,Pichon-Lesme, V.,Blessing, B.,Lecomte, C. (deposition date: 2000-03-02, release date: 2000-04-05, Last modification date: 2024-10-30)

Primary citation

Jelsch, C.,Teeter, M.M.,Lamzin, V.,Pichon-Pesme, V.,Blessing, R.H.,Lecomte, C.
Accurate protein crystallography at ultra-high resolution: valence electron distribution in crambin.
Proc.Natl.Acad.Sci.USA, 97:3171-3176, 2000

PubMed 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.

PubMed: 10737790
DOI: 10.1073/pnas.97.7.3171

Experimental method

X-RAY DIFFRACTION (0.54 Å)