Cloning, expression, purification, crystallization and initial crystallographic analysis of the preprotein translocation ATPase SecA fromThermus thermophilus
- 18 August 2006
- journal article
- crystallization communications
- Published by International Union of Crystallography (IUCr) in Acta Crystallographica Section F Structural Biology and Crystallization Communications
- Vol. 62 (9) , 909-912
- https://doi.org/10.1107/s1744309106030843
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 P31(2)21 (a = b = 168.6, c = 149.8 Å) and P61(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.Keywords
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