Open AccessCloning, expression, purification, crystallization and preliminary X‐ray crystallographic study of molybdopterin synthase from Thermus thermophilus HB8
Author(s) -
Ohmori Miwa,
Ranjani Chellamuthu Vasuki,
Kanaujia Shankar Prasad,
Jeyakanthan Jeyaraman,
Agari Kazuko,
Baba Seiki,
Ebihara Akio,
Kitamura Yoshiaki,
Shiro Yoshitsugu,
Shinkai Akeo,
Kuramitsu Seiki,
Sekar Kanagaraj,
Yokoyama Shigeyuki
Publication year - 2007
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309107011426
Subject(s) - thermus thermophilus , cloning (programming) , crystallization , crystallography , atp synthase , chemistry , materials science , biochemistry , enzyme , gene , escherichia coli , organic chemistry , computer science , programming language
Thermus thermophilus is a Gram‐negative aerobic thermophilic eubacterium which can grow at temperatures ranging from 323 to 355 K. In addition to their importance in thermostability or adaptation strategies for survival at high temperatures, the thermostable enzymes in thermophilic organisms contribute to a wide range of biotechnological applications. The molybdenum cofactor in all three kingdoms consists of a tricyclic pyranopterin termed molybdopterin that bears the cis ‐dithiolene group responsible for molybdenum ligation. The crystals of molybdopterin synthase from T. thermophilus HB8 belong to the primitive monoclinic space group P 2 1 , with unit‐cell parameters a = 33.94, b = 103.32, c = 59.59 Å, β = 101.3°. Preliminary studies and molecular‐replacement calculations reveal the presence of three monomers in the asymmetric unit.