5VNQ

Neutron crystallographic structure of perdeuterated T4 lysozyme cysteine-free pseudo-wild type at cryogenic temperature

5VNQ の概要

• エントリーDOI: 10.2210/pdb5vnq/pdb
• 関連するPDBエントリー: 5VNR
• 分子名称: Endolysin, CHLORIDE ION (3 entities in total)
• 機能のキーワード: t4 lysozyme, neutron crystallography, hydrogen bonding network, hydrogen bond, water, hydrolase
• 由来する生物種: Enterobacteria phage T4
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 18699.27

構造登録者

Li, L.,Shukla, S.,Meilleur, F.,Standaert, R.F.,Pierce, J.,Myles, D.A.A.,Cuneo, M.J. (登録日: 2017-05-01, 公開日: 2017-07-26, 最終更新日: 2023-10-04)

主引用文献

Li, L.,Shukla, S.,Meilleur, F.,Standaert, R.F.,Pierce, J.,Myles, D.A.A.,Cuneo, M.J.
Neutron crystallographic studies of T4 lysozyme at cryogenic temperature.
Protein Sci., 26:2098-2104, 2017

PubMed Abstract: Bacteriophage T4 lysozyme (T4L) has been used as a paradigm for seminal biophysical studies on protein structure, dynamics, and stability. Approximately 700 mutants of this protein and their respective complexes have been characterized by X-ray crystallography; however, despite the high resolution diffraction limits attained in several studies, no hydrogen atoms were reported being visualized in the electron density maps. To address this, a 2.2 Å-resolution neutron data set was collected at 80 K from a crystal of perdeuterated T4L pseudo-wild type. We describe a near complete atomic structure of T4L, which includes the positions of 1737 hydrogen atoms determined by neutron crystallography. The cryogenic neutron model reveals explicit detail of the hydrogen bonding interactions in the protein, in addition to the protonation states of several important residues.

PubMed: 28707382
DOI: 10.1002/pro.3231

実験手法

NEUTRON DIFFRACTION (2.2 Å)