Open AccessCrystallization and X‐ray diffraction analysis of 6‐aminohexanoate‐cyclic‐dimer hydrolase from Arthrobacter sp. KI72
Author(s) -
Yasuhira Kengo,
Uedo Yuki,
Shibata Naoki,
Negoro Seiji,
Takeo Masahiro,
Higuchi Yoshiki
Publication year - 2006
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309106045076
Subject(s) - dimer , arthrobacter , crystallization , imidazole , chemistry , hydrolase , crystallography , derivative (finance) , nuclear chemistry , stereochemistry , enzyme , organic chemistry , financial economics , economics
6‐Aminohexanoate‐cyclic‐dimer hydrolase (EI) from Arthrobacter sp. KI72 was expressed in Escherichia coli and purified by anion‐exchange chromatography. EI was crystallized by the sitting‐drop vapour‐diffusion method with sodium citrate as precipitant in imidazole buffer pH 8.0. The crystal is hexagonal, with unit‐cell parameters a = b = 130.75, c = 58.23 Å. Diffraction data were collected from native and mercury(II) dichloride‐derivative crystals to resolutions of 1.90 and 2.06 Å, respectively.