Open AccessPreparation, crystallization and preliminary X‐ray crystallographic studies of diadenosine tetraphosphate hydrolase from Shigella flexneri 2a
Author(s) -
Hu Wenxin,
Wang Qihai,
Bi Ruchang
Publication year - 2005
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s174430910503722x
Subject(s) - hydrolase , shigella flexneri , escherichia coli , chemistry , crystallization , enzyme , biology , biochemistry , microbiology and biotechnology , organic chemistry , gene
Diadenosine tetraphosphate (Ap 4 A) hydrolase (EC 3.6.1.41) hydrolyzes Ap 4 A symmetrically in prokaryotes. It plays a potential role in organisms by regulating the concentration of Ap 4 A in vivo . To date, no three‐dimensional structures of proteins with significant sequence homology to this protein have been determined. The 31.3 kDa Ap 4 A hydrolase from Shigella flexneri 2a has been cloned, expressed and purified using an Escherichia coli expression system. Crystals of Ap 4 A hydrolase have been obtained by the hanging‐drop technique at 291 K using PEG 550 MME as precipitant. Ap 4 A hydrolase crystals diffract X‐rays to 3.26 Å and belong to space group P 2 1 , with unit‐cell parameters a = 118.9, b = 54.6, c = 128.5 Å, β = 95.7°.