5WR8

Thaumatin structure determined by SACLA at 1.55 Angstrom

5WR8 の概要

• エントリーDOI: 10.2210/pdb5wr8/pdb
• 分子名称: Thaumatin I, L(+)-TARTARIC ACID (3 entities in total)
• 機能のキーワード: sweet-tasting protein, sweet receptor, 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: 22378.13

構造登録者

Masuda, T.,Suzuki, M.,Inoue, S.,Sugahara, M. (登録日: 2016-12-01, 公開日: 2017-11-29, 最終更新日: 2024-10-23)

主引用文献

Sugahara, M.,Nakane, T.,Masuda, T.,Suzuki, M.,Inoue, S.,Song, C.,Tanaka, R.,Nakatsu, T.,Mizohata, E.,Yumoto, F.,Tono, K.,Joti, Y.,Kameshima, T.,Hatsui, T.,Yabashi, M.,Nureki, O.,Numata, K.,Nango, E.,Iwata, S.
Hydroxyethyl cellulose matrix applied to serial crystallography
Sci Rep, 7:703-703, 2017

PubMed Abstract: Serial femtosecond crystallography (SFX) allows structures of proteins to be determined at room temperature with minimal radiation damage. A highly viscous matrix acts as a crystal carrier for serial sample loading at a low flow rate that enables the determination of the structure, while requiring consumption of less than 1 mg of the sample. However, a reliable and versatile carrier matrix for a wide variety of protein samples is still elusive. Here we introduce a hydroxyethyl cellulose-matrix carrier, to determine the structure of three proteins. The de novo structure determination of proteinase K from single-wavelength anomalous diffraction (SAD) by utilizing the anomalous signal of the praseodymium atom was demonstrated using 3,000 diffraction images.

PubMed: 28386083
DOI: 10.1038/s41598-017-00761-0

実験手法

X-RAY DIFFRACTION (1.55 Å)