Open AccessCrystallization and X‐ray diffraction analysis of 6‐aminohexanoate‐dimer hydrolase from Arthrobacter sp. KI72
Author(s) -
Ohki Taku,
Mizuno Nobuhiro,
Shibata Naoki,
Takeo Masahiro,
Negoro Seiji,
Higuchi Yoshiki
Publication year - 2005
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309105028812
Subject(s) - arthrobacter , crystallization , dimer , crystallography , diffraction , x ray crystallography , materials science , x ray , chemistry , physics , optics , enzyme , biochemistry , organic chemistry
To investigate the structure–function relationship between 6‐aminohexanoate‐dimer hydrolase (EII) from Arthrobacter sp. and a cryptic protein (EII′) which shows 88% sequence identity to EII, a hybrid protein (named Hyb‐24) of EII and EII′ was overexpressed, purified and crystallized using the sitting‐drop vapour‐diffusion method with ammonium sulfate as a precipitant in MES buffer pH 6.5. The crystal belongs to space group P 3 1 21 or P 3 2 21, with unit‐cell parameters a = b = 96.37, c = 113.09 Å. Diffraction data were collected from native and methylmercuric chloride derivative crystals to resolutions of 1.75 and 1.80 Å, respectively.