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Crystallization of acetate kinase from Methanosarcina thermophila and prediction of its fold.
The unique biochemical properties of acetate kinase present a classic conundrum in the study of the mechanism of enzyme-catalyzed phosphoryl transfer. Large, single crystals of acetate kinase from Methanosarcina thermophila were grown from a solution of ammonium sulfate in the presence of ATP. The c...
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| Autores principales: | , , , , |
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| Formato: | Artigo |
| Lenguaje: | Inglês |
| Publicado: |
Cold Spring Harbor Laboratory Press
1997
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| Materias: | |
| Acceso en línea: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2143604/ https://ncbi.nlm.nih.gov/pubmed/9416619 |
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