Kim Jieun, Kim Kyung-Jin
School of Life Sciences, KNU Creative BioResearch Group (BK21 plus program), Kyungpook National University, Daehak-ro 80, Buk-ku, Daegu 702-701, Republic of Korea.
Acta Crystallogr F Struct Biol Commun. 2014 Jul;70(Pt 7):955-8. doi: 10.1107/S2053230X14011881. Epub 2014 Jun 19.
The (S)-3-hydroxybutyryl-CoA dehydrogenase PaaH1 from Ralstonia eutropha (RePaaH1) is an enzyme used in the biosynthesis of n-butanol from acetyl-CoA by the reduction of acetoacetyl-CoA to (S)-3-hydroxybutyryl-CoA. The RePaaH1 protein was crystallized using the hanging-drop vapour-diffusion method in the presence of 1.4 M ammonium sulfate, 0.1 M sodium cacodylate pH 6.0, 0.2 M sodium chloride at 295 K. X-ray diffraction data were collected to a maximum resolution of 2.6 Å on a synchrotron beamline. The crystal belonged to space group P3221, with unit-cell parameters a=b=135.4, c=97.2 Å. With three molecules per asymmetric unit, the crystal volume per unit protein weight (VM) is 2.68 Å3 Da(-1), which corresponds to a solvent content of approximately 54.1%. The structure was solved by the single-wavelength anomalous dispersion method and refinement of the structure is in progress.
来自真养产碱菌的（S）-3-羟基丁酰辅酶A脱氢酶PaaH1（RePaaH1）是一种通过将乙酰乙酰辅酶A还原为（S）-3-羟基丁酰辅酶A，用于从乙酰辅酶A生物合成正丁醇的酶。RePaaH1蛋白采用悬滴气相扩散法，在1.4 M硫酸铵、0.1 M pH 6.0的二甲胂酸钠、0.2 M氯化钠存在的条件下，于295 K结晶。在同步加速器光束线上收集到最大分辨率为2.6 Å的X射线衍射数据。晶体属于P3221空间群，晶胞参数a = b = 135.4，c = 97.2 Å。每个不对称单元有三个分子，每单位蛋白质重量的晶体体积（VM）为2.68 Å3 Da-1，对应溶剂含量约为54.1%。该结构通过单波长反常色散法解析，结构精修正在进行中。
