2XHY

Crystal Structure of E.coli BglA

2XHY の概要

• エントリーDOI: 10.2210/pdb2xhy/pdb
• 分子名称: 6-PHOSPHO-BETA-GLUCOSIDASE BGLA, BROMIDE ION, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: hydrolase, glycosidase
• 由来する生物種: ESCHERICHIA COLI
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 223708.85

構造登録者

Totir, M.,Zubieta, C.,Echols, N.,May, A.P.,Gee, C.L.,nanao, M.,alber, T. (登録日: 2010-06-24, 公開日: 2011-07-06, 最終更新日: 2023-12-20)

主引用文献

Totir, M.,Echols, N.,Nanao, M.,Gee, C.L.,Moskaleva, A.,Gradia, S.,Iavarone, A.T.,Berger, J.M.,May, A.P.,Zubieta, C.,Alber, T.
Macro-to-Micro Structural Proteomics: Native Source Proteins for High-Throughput Crystallization.
Plos One, 7:32498-, 2012

PubMed Abstract: Structural biology and structural genomics projects routinely rely on recombinantly expressed proteins, but many proteins and complexes are difficult to obtain by this approach. We investigated native source proteins for high-throughput protein crystallography applications. The Escherichia coli proteome was fractionated, purified, crystallized, and structurally characterized. Macro-scale fermentation and fractionation were used to subdivide the soluble proteome into 408 unique fractions of which 295 fractions yielded crystals in microfluidic crystallization chips. Of the 295 crystals, 152 were selected for optimization, diffraction screening, and data collection. Twenty-three structures were determined, four of which were novel. This study demonstrates the utility of native source proteins for high-throughput crystallography.

PubMed: 22393408
DOI: 10.1371/JOURNAL.PONE.0032498

実験手法

X-RAY DIFFRACTION (2.3 Å)