期刊
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY
卷 57, 期 -, 页码 1887-1889出版社
INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S0907444901015189
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Glucose dehydrogenase (E.C 1.1.1.47; GlcDH) from Haloferax mediterranei has been overexpressed in Escherichia coli, solubilized by the addition of 8 M urea and refolded by rapid dilution. The protein has been purified by conventional techniques and crystallized by the hanging-drop vapour-diffusion method using sodium citrate as the precipitant. Two crystal forms representing the free enzyme and the binary complex with NADP(+) grow under these conditions. Crystals of form I diffract to beyond 3.5 Angstrom resolution and belong to the hexagonal space group P622, with unit-cell parameters a=b=89.1, c=214.6 Angstrom, alpha=beta =90, gamma =120 degrees. Crystals of form II diffract to greater than 2.0 Angstrom and belong to the orthorhombic space group I222 or I2(1)2(1)2(1), with unit-cell parameters a=61.8, b=110.9, c=151.7 Angstrom, alpha=beta=gamma =90 degrees. Calculated values for V-M and consideration of the packing for both crystal forms suggests that the asymmetric units in both crystal forms contain a monomer.
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