6G89

Thaumatin solved by Native SAD from a dataset collected in 0.6 second with JUNGFRAU detector

6G89 の概要

• エントリーDOI: 10.2210/pdb6g89/pdb
• 分子名称: Thaumatin I, L(+)-TARTARIC ACID (3 entities in total)
• 機能のキーワード: native-sad, jungfrau, integrating detector, 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: 22457.14

構造登録者

Leonarski, F.,Olieric, V.,Vera, L.,Redford, S.,Wang, M. (登録日: 2018-04-08, 公開日: 2018-08-01, 最終更新日: 2024-10-23)

主引用文献

Leonarski, F.,Redford, S.,Mozzanica, A.,Lopez-Cuenca, C.,Panepucci, E.,Nass, K.,Ozerov, D.,Vera, L.,Olieric, V.,Buntschu, D.,Schneider, R.,Tinti, G.,Froejdh, E.,Diederichs, K.,Bunk, O.,Schmitt, B.,Wang, M.
Fast and accurate data collection for macromolecular crystallography using the JUNGFRAU detector.
Nat. Methods, 15:799-804, 2018

PubMed Abstract: The accuracy of X-ray diffraction data is directly related to how the X-ray detector records photons. Here we describe the application of a direct-detection charge-integrating pixel-array detector (JUNGFRAU) in macromolecular crystallography (MX). JUNGFRAU features a uniform response on the subpixel level, linear behavior toward high photon rates, and low-noise performance across the whole dynamic range. We demonstrate that these features allow accurate MX data to be recorded at unprecedented speed. We also demonstrate improvements over previous-generation detectors in terms of data quality, using native single-wavelength anomalous diffraction (SAD) phasing, for thaumatin, lysozyme, and aminopeptidase N. Our results suggest that the JUNGFRAU detector will substantially improve the performance of synchrotron MX beamlines and equip them for future synchrotron light sources.

PubMed: 30275593
DOI: 10.1038/s41592-018-0143-7

実験手法

X-RAY DIFFRACTION (2.359 Å)