Crystallization and X-ray diffraction analysis of 6-aminohexanoate-dimer hydrolase from Arthrobacter sp. KI72.
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 P3(1)21 or P3(2)21, with unit-cell parameters a = b = 96.37, c = 113.09 A. Diffraction data were collected from native and methylmercuric chloride derivative crystals to resolutions of 1.75 and 1.80 A, respectively.
Ohki
Taku
T
Department of Materials Science and Chemistry, Graduate School of Engineering, University of Hyogo, 2167 Shosha, Himeji, Hyogo 671-2201, Japan.
Mizuno
Nobuhiro
N
Shibata
Naoki
N
Takeo
Masahiro
M
Negoro
Seiji
S
Higuchi
Yoshiki
Y
D000581:Amidohydrolases / Q000737:chemistry*; D000645:Ammonium Sulfate / Q000737:chemistry; D001173:Arthrobacter / Q000378:metabolism*; D001673:Biodegradation, Environmental; D003460:Crystallization; D018360:Crystallography, X-Ray; D004058:Diffusion; D019281:Dimerization; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D009757:Nylons / Q000737:chemistry; D010957:Plasmids / Q000378:metabolism; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D013329:Structure-Activity Relationship; D014961:X-Ray Diffraction
D009757:Nylons; D000581:Amidohydrolases; C026250:6-aminohexanoate-dimer hydrolase; D000645:Ammonium Sulfate