Yasutake Yoshiaki, Nishiya Yoshiaki, Tamura Noriko, Tamura Tomohiro
Research Institute of Genome-based Biofactory, National Institute of Advanced Industrial Science and Technology (AIST), 2-17-2-1 Tsukisamu-Higashi, Toyohira-ku, Sapporo 062-8517, Japan.
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Jun 1;62(Pt 6):586-9. doi: 10.1107/S1744309106017362. Epub 2006 May 31.
The aldohexose dehydrogenase from the thermoacidophilic archaeon Thermoplasma acidophilum (AldT) is a 28 kDa molecular-weight enzyme that catalyzes the oxidation of various aldohexoses, with a preference for NAD+ rather than NADP+ as a cofactor. The recombinant AldT was crystallized using the hanging-drop vapour-diffusion technique at 293 K under several acidic conditions with polyethylene glycol (PEG) and ammonium sulfate as precipitants. Optimization of the initial crystallizations conditions yielded single crystals in solution containing 0.1 M sodium acetate pH 4.6, 18%(w/v) PEG 4000, 0.2 M ammonium sulfate and 15%(v/v) glycerol. An X-ray diffraction data set was collected to a resolution of 2.8 A.
嗜热嗜酸古菌嗜热栖热菌（Thermoplasma acidophilum）的醛己糖脱氢酶（AldT）是一种分子量为28 kDa的酶，可催化各种醛己糖的氧化反应，其辅因子偏好NAD⁺而非NADP⁺。重组AldT采用悬滴气相扩散技术，于293 K下在几种酸性条件下，以聚乙二醇（PEG）和硫酸铵作为沉淀剂进行结晶。对初始结晶条件进行优化后，在含有0.1 M乙酸钠（pH 4.6）、18%（w/v）PEG 4000、0.2 M硫酸铵和15%（v/v）甘油的溶液中获得了单晶。收集到了分辨率为2.8 Å的X射线衍射数据集。
