Crystallization of the regulatory and effector domains of the key sporulation response regulator Spo0A
| Autor: | Wendy A. Offen, Anthony J. Wilkinson, Philip Youngman, Katarína Muchová, James A. Brannigan, Richard J. Lewis, David Brown, Imrich Barák |
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| Rok vydání: | 1999 |
| Předmět: |
Protein Conformation
Molecular Sequence Data Biology Crystallography X-Ray law.invention Geobacillus stearothermophilus 03 medical and health sciences Protein structure Bacterial Proteins Structural Biology law Amino Acid Sequence Cloning Molecular Crystallization Peptide sequence Gene Transcription factor 030304 developmental biology 0303 health sciences Sequence Homology Amino Acid Effector Hydrolysis fungi 030302 biochemistry & molecular biology General Medicine Spore Response regulator Biochemistry Biophysics bacteria Transcription Factors |
| Zdroj: | Acta Crystallographica Section D Biological Crystallography. 55:671-676 |
| ISSN: | 0907-4449 |
| DOI: | 10.1107/s0907444998012682 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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