High speed X-ray analysis of plant enzymes at room temperature

被引：2

作者：

Xia, Liqun ^{[1
]}

Rajendran, Chitra ^{[2
]}

Ruppert, Martin ^{[3
]}

Panjikar, Santosh ^{[4
]}

Wang, Meitian ^{[2
]}

Stoeckigt, Joachim ^{[1
]}

机构：

[1] Zhejiang Univ, Coll Pharmaceut Sci, Inst Mat Med, Hangzhou 310058, Zhejiang, Peoples R China

[2] Paul Scherrer Inst, Swiss Light Source, CH-5232 Villigen, Switzerland

[3] Johannes Gutenberg Univ Mainz, Inst Pharm & Biochem, D-55099 Mainz, Germany

[4] Hamburg Outstn Deutsch Elektronen Synchrotron, European Mol Biol Lab, D-22603 Hamburg, Germany

来源：

PHYTOCHEMISTRY | 2013年 / 91卷

关键词：

Rauvolfia serpentina (L.) Benth; Apocynaceae; Raucaffricine-O-beta-D-glucosidase; Enzyme crystal structures; Ligand complexes; X-ray diffraction; Room temperature; High speed measurements; RADIATION-DAMAGE; PILATUS; GLUCOSIDASE; EXPRESSION;

D O I：

10.1016/j.phytochem.2012.05.009

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

X-ray measurements at room temperature (295 K) deliver high quality data sets with unprecedented speed (<2 min), as shown for crystallized raucaffricine-O-beta-D-glucosidase (RG), its mutant RG-Glu186Gln and several ligand complexes of the enzyme which participates in alkaloid biosynthesis in the plant Rauvolfia. The data obtained are compared with data sets measured under typical cryo conditions (100 K). Under both conditions, density maps are highly comparable and favor the described protocol for room temperature measurements, potentially paving the way for future crystallographic studies capturing biosynthetic pathway intermediates. Crown Copyright (C) 2012 Published by Elsevier Ltd. All rights reserved.

引用

页码：88 / 92

页数：5

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