6S19

Structure of thaumatin determined at SwissFEL using native-SAD at 4.57 keV from all available diffraction patterns

6S19 の概要

• エントリーDOI: 10.2210/pdb6s19/pdb
• 関連するPDBエントリー: 6s0l 6s0q
• 分子名称: Thaumatin-1, L(+)-TARTARIC ACID (2 entities in total)
• 機能のキーワード: native-sad, serial femtosecond crystallography, sfx, swissfel, jungfrau, plant protein
• 由来する生物種: Thaumatococcus daniellii (Katemfe)
• 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.,Cheng, R.,Vera, L.,Mozzanica, A.,Redford, S.,Ozerov, D.,Basu, S.,James, D.,Knopp, G.,Cirelli, C.,Martiel, I.,Casadei, C.,Weinert, T.,Nogly, P.,Skopintsev, P.,Usov, I.,Leonarski, F.,Geng, T.,Rappas, M.,Dore, A.S.,Cooke, R.,Nasrollahi Shirazi, S.,Dworkowski, F.,Sharpe, M.,Olieric, N.,Steinmetz, M.O.,Schertler, G.,Abela, R.,Patthey, L.,Schmitt, B.,Hennig, M.,Standfuss, J.,Wang, M.,Milne, J.Ch. (登録日: 2019-06-18, 公開日: 2020-07-15, 最終更新日: 2024-11-13)

主引用文献

Nass, K.,Cheng, R.,Vera, L.,Mozzanica, A.,Redford, S.,Ozerov, D.,Basu, S.,James, D.,Knopp, G.,Cirelli, C.,Martiel, I.,Casadei, C.,Weinert, T.,Nogly, P.,Skopintsev, P.,Usov, I.,Leonarski, F.,Geng, T.,Rappas, M.,Dore, A.S.,Cooke, R.,Nasrollahi Shirazi, S.,Dworkowski, F.,Sharpe, M.,Olieric, N.,Bacellar, C.,Bohinc, R.,Steinmetz, M.O.,Schertler, G.,Abela, R.,Patthey, L.,Schmitt, B.,Hennig, M.,Standfuss, J.,Wang, M.,Milne, C.J.
Advances in long-wavelength native phasing at X-ray free-electron lasers.
Iucrj, 7:965-975, 2020

PubMed Abstract: Long-wavelength pulses from the Swiss X-ray free-electron laser (XFEL) have been used for protein structure determination by native single-wavelength anomalous diffraction (native-SAD) phasing of serial femtosecond crystallography (SFX) data. In this work, sensitive anomalous data-quality indicators and model proteins were used to quantify improvements in native-SAD at XFELs such as utilization of longer wavelengths, careful experimental geometry optimization, and better post-refinement and partiality correction. Compared with studies using shorter wavelengths at other XFELs and older software versions, up to one order of magnitude reduction in the required number of indexed images for native-SAD was achieved, hence lowering sample consumption and beam-time requirements significantly. Improved data quality and higher anomalous signal facilitate so-far underutilized structure determination of challenging proteins at XFELs. Improvements presented in this work can be used in other types of SFX experiments that require accurate measurements of weak signals, for example time-resolved studies.

PubMed: 33209311
DOI: 10.1107/S2052252520011379

実験手法

X-RAY DIFFRACTION (2.65 Å)