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Updated: Jul 20, 2026

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050
Published on: May 13, 2020
Cloning, expression, purification, crystallization and initial crystallographic analysis of the preprotein
Marina N Vassylyeva1, Hiroyuki Mori, Tomoya Tsukazaki
1Department of Biochemistry and Molecular Genetics, University of Alabama at Birmingham, 402B Kaul Genetics Building, 720 20th Street South, Birmingham, AL 35294, USA.
Abstract:
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 P3(1(2))21 (a = b = 168.6, c = 149.8 A) and P6(1(5))22 (a = b = 130.9, c = 564.6 A). The crystals, improved by macroseeding, diffracted to beyond 2.8 and 3.5 A resolution for the trigonal and hexagonal crystal forms, respectively. Structure determination using the multiple isomorphous replacement method is in progress.
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