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Crystallization and preliminary X-ray diffraction analysis of the α subdomain of Lon protease from Brevibacillus thermoruber
DNA-binding ability has previously been reported as a novel function for the thermostable Lon protease from Brevibacillus thermoruber WR-249 (Bt-Lon), and the α subdomain (amino acids 491–605) of Bt-Lon has been identified as being responsible for DNA binding. However, the physiological role and DNA...
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| Main Authors: | , , , |
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| Formato: | Artigo |
| Idioma: | Inglês |
| Publicado em: |
International Union of Crystallography
2013
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| Assuntos: | |
| Acesso em linha: | https://ncbi.nlm.nih.gov/pmc/articles/PMC3729169/ https://ncbi.nlm.nih.gov/pubmed/23908038 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1107/S1744309113017958 |
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