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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Adenosine Triphosphatases / biosynthesis
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Adenosine Triphosphatases / chemistry*
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Adenosine Triphosphatases / genetics*
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Bacterial Proteins / biosynthesis
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Bacterial Proteins / chemistry*
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Bacterial Proteins / genetics*
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Cloning, Molecular
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Crystallization
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Crystallography, X-Ray / methods
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Membrane Transport Proteins / biosynthesis
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Membrane Transport Proteins / chemistry*
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Membrane Transport Proteins / genetics*
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Protein Precursors / biosynthesis
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Protein Precursors / chemistry
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Protein Precursors / genetics
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SEC Translocation Channels
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SecA Proteins
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Thermus thermophilus / enzymology*
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Thermus thermophilus / genetics*
Substances
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Bacterial Proteins
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Membrane Transport Proteins
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Protein Precursors
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SEC Translocation Channels
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Adenosine Triphosphatases
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SecA Proteins