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 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.
|Original language||English (US)|
|Number of pages||4|
|Journal||Acta Crystallographica Section F: Structural Biology and Crystallization Communications|
|Publication status||Published - Sep 1 2006|
ASJC Scopus subject areas
- Structural Biology
- Condensed Matter Physics