Cloning, expression, purification, crystallization and initial crystallographic analysis of the preprotein translocation ATPase SecA from Thermus thermophilus.
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.
Vassylyeva
Marina N
MN
Department of Biochemistry and Molecular Genetics, University of Alabama at Birmingham, 402B Kaul Genetics Building, 720 20th Street South, Birmingham, AL 35294, USA.
Mori
Hiroyuki
H
Tsukazaki
Tomoya
T
Yokoyama
Shigeyuki
S
Tahirov
Tahir H
TH
Ito
Koreaki
K
Vassylyev
Dmitry G
DG
D000251:Adenosine Triphosphatases / Q000096:biosynthesis / Q000737:chemistry* / Q000235:genetics*; D001426:Bacterial Proteins / Q000096:biosynthesis / Q000737:chemistry* / Q000235:genetics*; D003001:Cloning, Molecular; D003460:Crystallization; D018360:Crystallography, X-Ray / Q000379:methods; D026901:Membrane Transport Proteins / Q000096:biosynthesis / Q000737:chemistry* / Q000235:genetics*; D011498:Protein Precursors / Q000096:biosynthesis / Q000737:chemistry / Q000235:genetics; D000069816:SEC Translocation Channels; D000081416:SecA Proteins; D016963:Thermus thermophilus / Q000201:enzymology* / Q000235:genetics*
D001426:Bacterial Proteins; D026901:Membrane Transport Proteins; D011498:Protein Precursors; D000069816:SEC Translocation Channels; D000251:Adenosine Triphosphatases; D000081416:SecA Proteins