1IO5

HYDROGEN AND HYDRATION OF HEN EGG-WHITE LYSOZYME DETERMINED BY NEUTRON DIFFRACTION

1IO5 の概要

• エントリーDOI: 10.2210/pdb1io5/pdb
• 分子名称: LYSOZYME C (2 entities in total)
• 機能のキーワード: hydrogen, hydration, hydrolase
• 由来する生物種: Gallus gallus (chicken)
• 細胞内の位置: Secreted: P00698
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 14331.16

構造登録者

Niimura, N.,Minezaki, Y.,Nonaka, T.,Castagna, J.C.,Cipriani, F.,Hoeghoej, P.,Lehmann, M.S.,Wilkinson, C. (登録日: 2001-01-14, 公開日: 2001-02-07, 最終更新日: 2024-10-16)

主引用文献

Niimura, N.,Minezaki, Y.,Nonaka, T.,Castagna, J.C.,Cipriani, F.,Hoghoj, P.,Lehmann, M.S.,Wilkinson, C.
Neutron Laue diffractometry with an imaging plate provides an effective data collection regime for neutron protein crystallography.
Nat.Struct.Biol., 4:909-914, 1997

PubMed Abstract: Neutron quasi-Laue diffraction data (2 A resolution) from tetragonal hen egg-white lysozyme were collected in ten days with neutron imaging plates. The data processing Laue software, LAUEGEN, developed for X-ray Laue diffractometry, was adapted for neutron diffractometry with a cylindrical detector. The data analysis software, X-PLOR, was modified and used for the refinement of hydrogen atoms, and the positions of 960 hydrogen atoms in the protein and 157 bound water molecules, were determined. Several examples are given of the methods used to identify hydrogen atoms and water molecules.

PubMed: 9360606
DOI: 10.1038/nsb1197-909

実験手法

NEUTRON DIFFRACTION (2 Å)