5LMH

High dose Thaumatin - 160-200 ms.

5LMH の概要

• エントリーDOI: 10.2210/pdb5lmh/pdb
• 分子名称: Thaumatin-1, L(+)-TARTARIC ACID (3 entities in total)
• 機能のキーワード: multicrystal, room-temperature, thaumatin, 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: 22527.23

構造登録者

Schubert, R.,Kapis, S.,Heymann, M.,Giquel, Y.,Bourenkov, G.,Schneider, T.,Betzel, C.,Perbandt, M. (登録日: 2016-07-30, 公開日: 2016-11-09, 最終更新日: 2024-10-16)

主引用文献

Schubert, R.,Kapis, S.,Gicquel, Y.,Bourenkov, G.,Schneider, T.R.,Heymann, M.,Betzel, C.,Perbandt, M.
A multicrystal diffraction data-collection approach for studying structural dynamics with millisecond temporal resolution.
IUCrJ, 3:393-401, 2016

PubMed Abstract: Many biochemical processes take place on timescales ranging from femto-seconds to seconds. Accordingly, any time-resolved experiment must be matched to the speed of the structural changes of interest. Therefore, the timescale of interest defines the requirements of the X-ray source, instrumentation and data-collection strategy. In this study, a minimalistic approach for crystallization is presented that requires only a few microlitres of sample solution containing a few hundred crystals. It is demonstrated that complete diffraction data sets, merged from multiple crystals, can be recorded within only a few minutes of beamtime and allow high-resolution structural information of high quality to be obtained with a temporal resolution of 40 ms. Global and site-specific radiation damage can be avoided by limiting the maximal dose per crystal to 400 kGy. Moreover, analysis of the data collected at higher doses allows the time-resolved observation of site-specific radiation damage. Therefore, our approach is well suited to observe structural changes and possibly enzymatic reactions in the low-millisecond regime.

PubMed: 27840678
DOI: 10.1107/S2052252516016304

実験手法

X-RAY DIFFRACTION (1.96 Å)