Crystallization of acetate kinase from Methanosarcina thermophila and prediction of its fold

Kathryn A. Buss, Cheryl Ingram-Smith, James G. Ferry, David A. Sanders, Miriam S. Hasson

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23 Scopus citations


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 crystals diffract to beyond 1.7 Å resolution. Analysis of X-ray data from the crystals is consistent with a space group of C2 and unit cell dimensions a = 181 Å, b = 67 Å, c = 83 Å, β = 103°. Diffraction data have been collected from the crystals at 110 and 277 K. Data collected at 277 K extend to lower resolution, but are more reproducible. The orientation of a noncrystallographic two-fold axis of symmetry has been determined. Based on an analysis of the predicted amino acid sequences of acetate kinase from several organisms, we hypothesize that acetate kinase is a member of the sugar kinase/actin/hsp70 structural family.

Original languageEnglish (US)
Pages (from-to)2659-2662
Number of pages4
JournalProtein Science
Issue number12
StatePublished - Dec 1997

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology


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