Cloning, expression, purification, crystallization and preliminary X-ray crystallographic study of molybdopterin synthase from Thermus thermophilus HB8

作者: Shankar Prasad Kanaujia , Chellamuthu Vasuki Ranjani , Jeyaraman Jeyakanthan , Miwa Ohmori , Kazuko Agari

DOI: 10.1107/S1744309107011426

关键词:

摘要: Thermus thermophilus is a Gram-negative aerobic thermophilic eubacterium which can grow at temperatures ranging from 323 to 355 K. In addition their importance in thermostability or adaptation strategies for survival high temperatures, the thermostable enzymes organisms contribute wide range of biotechnological applications. The molybdenum cofactor all three kingdoms consists tricyclic pyranopterin termed molybdopterin that bears cis-dithiolene group responsible ligation. crystals synthase T. HB8 belong primitive monoclinic space P21, with unit-cell parameters = 33.94, b = 103.32, c 59.59 A, β 101.3°. Preliminary studies and molecular-replacement calculations reveal presence monomers asymmetric unit.

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