Abstract
The key response-regulator gene of sporulation, spo0A, has been cloned from Bacillus stearothermophilus and the encoded protein purified. The DNA-binding and phospho-acceptor domains of Spo0A have been prepared by tryptic digestion of the intact protein and subsequently crystallized in forms suitable for X-ray crystallographic studies. The DNA-binding domain has been crystallized in two forms, one of which diffracts X-rays to beyond 2. 5 A spacing. The crystals of the phospho-acceptor domain diffract X-rays beyond 2.0 A spacing using synchrotron radiation.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acid Sequence
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Bacterial Proteins / chemistry*
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Bacterial Proteins / genetics
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Bacterial Proteins / isolation & purification
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Cloning, Molecular
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Crystallization
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Crystallography, X-Ray
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Geobacillus stearothermophilus / genetics
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Hydrolysis
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Molecular Sequence Data
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Protein Conformation
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Sequence Homology, Amino Acid
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Transcription Factors / chemistry*
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Transcription Factors / genetics
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Transcription Factors / isolation & purification
Substances
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Bacterial Proteins
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Spo0A protein, Bacillus subtilis
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Transcription Factors