5MF2

Bacteriophage T5 distal tail protein pb9 co-crystallized with Tb-Xo4

5MF2 の概要

• エントリーDOI: 10.2210/pdb5mf2/pdb
• 分子名称: Distal tail protein, TERBIUM(III) ION, Tb-Xo4, ... (5 entities in total)
• 機能のキーワード: lanthanide complexes, crystallogenesis, anomalous scattering, bacteriophages, viral protein
• 由来する生物種: Escherichia phage T5
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 101635.68

構造登録者

Engilberge, S.,Riobe, F.,Di Pietro, S.,Lassalle, L.,Arnaud, C.-A.,Breyton, C.,Madern, D.,Coquelle, N.,Maury, O.,Girard, E. (登録日: 2016-11-17, 公開日: 2017-09-20, 最終更新日: 2024-05-08)

主引用文献

Engilberge, S.,Riobe, F.,Di Pietro, S.,Lassalle, L.,Coquelle, N.,Arnaud, C.A.,Pitrat, D.,Mulatier, J.C.,Madern, D.,Breyton, C.,Maury, O.,Girard, E.
Crystallophore: a versatile lanthanide complex for protein crystallography combining nucleating effects, phasing properties, and luminescence.
Chem Sci, 8:5909-5917, 2017

PubMed Abstract: Macromolecular crystallography suffers from two major issues: getting well-diffracting crystals and solving the phase problem inherent to large macromolecules. Here, we describe the first example of a lanthanide complex family named "crystallophore" (Xo4), which contributes to tackling both bottlenecks. This terbium complex, Tb-Xo4, is an appealing agent for biocrystallography, combining the exceptional phasing power of the Tb(iii) heavy atom with powerful nucleating properties, providing ready-to-use crystals for structure determination. Furthermore, protein/Tb-Xo4 co-crystals can be easily detected and discriminated from other crystalline by-products using luminescence. We demonstrate the potential of this additive for the crystallisation and structure determination of eight proteins, two of whose structures were unknown.

PubMed: 29619195
DOI: 10.1039/c7sc00758b

実験手法

X-RAY DIFFRACTION (2 Å)