Acta Crystallographica Section F

Structural Biology and Crystallization Communications

Volume 61, Part 10 (October 2005)

crystallization communications

Acta Cryst. (2005). F61, 928-930 [ doi:10.1107/S1744309105028812 ]

Crystallization and X-ray diffraction analysis of 6-aminohexanoate-dimer hydrolase from Arthrobacter sp. KI72

T. Ohki, N. Mizuno, N. Shibata, M. Takeo, S. Negoro and Y. Higuchi

Abstract: 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 P3₁21 or P3₂21, 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.

Keywords: 6-aminohexanoate-dimer hydrolase; biodegradation; nylon oligomer.