Publisher： John Wiley & Sons Inc
E-ISSN： 1744-3091|61|10|928-930
ISSN： 1744-3091
Source： Acta Crystallographica Section F, Vol.61, Iss.10, 2005-10, pp. : 928-930
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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.
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