5FGX

Thaumatin solved by native sulphur SAD using synchrotron radiation

5FGX の概要

• エントリーDOI: 10.2210/pdb5fgx/pdb
• 分子名称: Thaumatin-1, L(+)-TARTARIC ACID (3 entities in total)
• 機能のキーワード: sulphur sad, synchrotron, plant protein
• 由来する生物種: Thaumatococcus daniellii (Katemfe)
• 細胞内の位置: Cytoplasmic vesicle: P02883
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 22377.15

構造登録者

Nass, K.J.,Meinhart, A.,Barends, T.R.M.,Foucar, L.,Gorel, A.,Aquila, A.,Botha, S.,Doak, R.B.,Koglin, J.,Liang, M.,Shoeman, R.L.,Williams, G.J.,Boutet, S.,Schlichting, I. (登録日: 2015-12-21, 公開日: 2016-06-08, 最終更新日: 2024-11-20)

主引用文献

Nass, K.,Meinhart, A.,Barends, T.R.,Foucar, L.,Gorel, A.,Aquila, A.,Botha, S.,Doak, R.B.,Koglin, J.,Liang, M.,Shoeman, R.L.,Williams, G.,Boutet, S.,Schlichting, I.
Protein structure determination by single-wavelength anomalous diffraction phasing of X-ray free-electron laser data.
Iucrj, 3:180-191, 2016

PubMed Abstract: Serial femtosecond crystallography (SFX) at X-ray free-electron lasers (XFELs) offers unprecedented possibilities for macromolecular structure determination of systems that are prone to radiation damage. However, phasing XFEL data de novo is complicated by the inherent inaccuracy of SFX data, and only a few successful examples, mostly based on exceedingly strong anomalous or isomorphous difference signals, have been reported. Here, it is shown that SFX data from thaumatin microcrystals can be successfully phased using only the weak anomalous scattering from the endogenous S atoms. Moreover, a step-by-step investigation is presented of the particular problems of SAD phasing of SFX data, analysing data from a derivative with a strong anomalous signal as well as the weak signal from endogenous S atoms.

PubMed: 27158504
DOI: 10.1107/S2052252516002980

実験手法

X-RAY DIFFRACTION (2.134 Å)