6F2M

Structure of the bacteriophage T5 distal tail protein pb9 co-crystallized with 10mM Tb-Xo4

6F2M の概要

• エントリーDOI: 10.2210/pdb6f2m/pdb
• 分子名称: Distal tail protein, Tb-Xo4, 1,2-ETHANEDIOL, ... (7 entities in total)
• 機能のキーワード: phage protein, crystallophore, tb-xo4, nucleation, phasing, lanthanide complexes, viral protein
• 由来する生物種: Escherichia phage T5 (Enterobacteria phage T5)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 100149.26

構造登録者

Engilberge, S.,Riobe, F.,Di Pietro, S.,Breyton, C.,Girard, E.,Dumont, E.,Maury, O. (登録日: 2017-11-24, 公開日: 2018-10-03, 最終更新日: 2024-05-08)

主引用文献

Engilberge, S.,Riobe, F.,Wagner, T.,Di Pietro, S.,Breyton, C.,Franzetti, B.,Shima, S.,Girard, E.,Dumont, E.,Maury, O.
Unveiling the Binding Modes of the Crystallophore, a Terbium-based Nucleating and Phasing Molecular Agent for Protein Crystallography.
Chemistry, 24:9739-9746, 2018

PubMed Abstract: Crystallophores are lanthanide complexes that act as powerful auxiliary for protein crystallography due to their strong nucleating and phasing effects. To get first insights on the mechanisms behind nucleation induced by Crystallophore, we systematically identified various elaborated networks of supramolecular interactions between Tb-Xo4 and subset of 6 protein structures determined by X-ray diffraction in complex with terbium-Crystallophore (Tb-Xo4). Such interaction mapping analyses demonstrate the versatile binding behavior of the Crystallophore and pave the way to a better understanding of its unique properties.

PubMed: 29806881
DOI: 10.1002/chem.201802172

実験手法

X-RAY DIFFRACTION (1.8 Å)