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首页> 外文期刊>Acta crystallographica, Section F. Structural biology and crystallization communications >Crystallization and preliminary X-ray characterization of an NAD(P)-dependent butanol dehydrogenase A from Geobacillus thermodenitrificans NG80-2
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Crystallization and preliminary X-ray characterization of an NAD(P)-dependent butanol dehydrogenase A from Geobacillus thermodenitrificans NG80-2

机译：嗜热芽孢杆菌NG80-2的NAD（P）依赖性丁醇脱氢酶A的结晶和初步X射线表征

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摘要

Geobacillus thermodenitrificans NG80-2 encodes two long-chain NAD(P)-dependent alcohol dehydrogenases, gtADH1 and gtADH2, in the terminal oxidation pathway of long-chain n-alkanes for the conversion of long-chain alkyl alcohols to their corresponding aldehydes. Both gtADH1 and gtADH2 are thermostable enzymes and oxidize long-chain alkyl alcohols up to at least C-30. In order to understand the structural basis for their role in long-chain alkane degradation, we have crystallized gtADH2. Single, colourless crystals were obtained from a recombinant preparation of ADH2 overexpressed in Escherichia coli. The crystals belong to space group C222(1), with unit-cell parameters a = 56.0, b = 99.6, c = 123.1 angstrom. Diffraction data were collected inhouse to 1.79 angstrom resolution. The crystals contain one monomer in the asymmetric unit, with a V-M value of 2.17 angstrom(3) Da(-1) and an estimated solvent content of 43%.
机译：地热芽孢杆菌NG80-2在长链正构烷烃的末端氧化途径中编码两个长链NAD（P）依赖性醇脱氢酶gtADH1和gtADH2，以将长链烷基醇转化为相应的醛。 gtADH1和gtADH2均为热稳定酶，可氧化长链烷基醇，直至至少C-30。为了了解其在长链烷烃降解中作用的结构基础，我们结晶了gtADH2。从在大肠杆菌中过表达的ADH2重组制剂中获得了无色晶体。晶体属于空间群C222（1），其晶胞参数a = 56.0，b = 99.6，c = 123.1埃。在内部以1.79埃的分辨率收集衍射数据。该晶体在不对称单元中包含一种单体，V-M值为2.17埃（3）Da（-1），估计的溶剂含量为43％。

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