1EJG

CRAMBIN AT ULTRA-HIGH RESOLUTION: VALENCE ELECTRON DENSITY.

1EJG の概要

• エントリーDOI: 10.2210/pdb1ejg/pdb
• 関連するPDBエントリー: 1AB1 1CBN 1CNR 1CRN
• 分子名称: CRAMBIN (PRO22,SER22/LEU25,ILE25) (1 entity in total)
• 機能のキーワード: valence electron density, multi-substate, multipole refinement, plant protein
• 由来する生物種: Crambe hispanica subsp. abyssinica
• 細胞内の位置: Secreted: P01542
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 4738.45

構造登録者

Jelsch, C.,Teeter, M.M.,Lamzin, V.,Pichon-Lesme, V.,Blessing, B.,Lecomte, C. (登録日: 2000-03-02, 公開日: 2000-04-05, 最終更新日: 2024-10-30)

主引用文献

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

実験手法

X-RAY DIFFRACTION (0.54 Å)