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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Bibliografiska uppgifter
Huvudupphovsmän: Buss, K. A., Ingram-Smith, C., Ferry, J. G., Sanders, D. A., Hasson, M. S.
Materialtyp: Artigo
Språk:Inglês
Publicerad: Cold Spring Harbor Laboratory Press 1997
Ämnen:
Research Article
Länkar:https://ncbi.nlm.nih.gov/pmc/articles/PMC2143604/
https://ncbi.nlm.nih.gov/pubmed/9416619
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