Open AccessCloning, expression, purification, crystallization and initial crystallographic analysis of the preprotein translocation ATPase SecA from Thermus thermophilus
Author(s) -
Vassylyeva Mari.,
Mori Hiroyuki,
Tsukazaki Tomoya,
Yokoyama Shigeyuki,
Tahirov Tahir H.,
Ito Koreaki,
Vassylyev Dmitry G.
Publication year - 2006
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309106030843
Subject(s) - thermus thermophilus , crystallization , crystallography , cloning (programming) , atpase , chemistry , biology , gene , microbiology and biotechnology , biochemistry , enzyme , escherichia coli , organic chemistry , computer science , programming language
The Thermus thermophilus gene encoding the preprotein translocation ATPase SecA was cloned and expressed and the purified protein was crystallized by the hanging‐drop vapour‐diffusion technique in two different space groups P 3 1(2) 21 ( a = b = 168.6, c = 149.8 Å) and P 6 1(5) 22 ( a = b = 130.9, c = 564.6 Å). The crystals, improved by macroseeding, diffracted to beyond 2.8 and 3.5 Å resolution for the trigonal and hexagonal crystal forms, respectively. Structure determination using the multiple isomorphous replacement method is in progress.