J. Biol. Chem., Vol. 265, Issue 29, 17413-17415, 10, 1990
Preliminary crystallographic data for the thiamin diphosphate-dependent enzyme pyruvate decarboxylase from brewers' yeast
F Dyda, W Furey, S Swaminathan, M Sax, B Farrenkopf and F Jordan
Biocrystallography Laboratory, VA Medical Center, Pittsburgh, Pennsylvania 15240.
Single crystals of the thiamin diphosphate (the vitamin B1 coenzyme)-
dependent enzyme pyruvate decarboxylase (EC 4.1.1.1) from brewers' yeast
have been grown using polyethylene glycol as a precipitating agent.
Crystals of the homotetrameric version alpha 4 of the holoenzyme are
triclinic, space group P1, with cell constants a = 81.0, b = 82.4, c =
116.6 A, alpha = 69.5 beta = 72.6, gamma = 62.4 degrees. The crystals are
reasonably stable in a rotating anode x-ray beam and diffract to at least
2.5 A resolution. The Vm value of 2.55 A/dalton is consistent with a unit
cell containing four subunits with mass of approximately 60 kDa each.
Rotation function results with native data indicate strong
non-crystallographic 222 symmetry relating the four identical subunits,
thus density averaging methods are likely to play a role in the structure
determination.
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