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• W2093534912 abstract "( S )-3-Hydroxybutyryl-CoA dehydrogenase from Clostridium butyricum ( Cb HBD) is an enzyme that catalyzes the second step in the biosynthesis of n -butanol from acetyl-CoA by the reduction of acetoacetyl-CoA to 3-hydroxybutyryl-CoA. The Cb HBD protein was crystallized using the hanging-drop vapour-diffusion method in the presence of 2 M ammonium sulfate, 0.1 M CAPS pH 10.5, 0.2 M lithium sulfate at 295 K. X-ray diffraction data were collected to a maximum resolution of 2.3 Å on a synchrotron beamline. The crystal belonged to space group R 3, with unit-cell parameters a = b = 148.5, c = 201.6 Å. With four molecules per asymmetric unit, the crystal volume per unit protein weight ( V M ) is 3.52 Å 3 Da −1 , which corresponds to a solvent content of approximately 65.04%. The structure was solved by the molecular-replacement method and refinement of the structure is in progress." @default.
• W2093534912 created "2016-06-24" @default.
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• W2093534912 creator A5091385586 @default.
• W2093534912 date "2014-03-25" @default.
• W2093534912 modified "2023-09-27" @default.
• W2093534912 title "Cloning, expression, purification, crystallization and X-ray crystallographic analysis of (<i>S</i>)-3-hydroxybutyryl-CoA dehydrogenase from<i>Clostridium butyricum</i>" @default.
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• W2093534912 doi "https://doi.org/10.1107/s2053230x14004348" @default.
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