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Title
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Preliminary crystallographic data for transketolase from yeast.
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Authors
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G.Schneider,
M.Sundström,
Y.Lindqvist.
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Ref.
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J Biol Chem, 1989,
264,
21619-21620.
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PubMed id
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Abstract
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Crystals of the vitamin B1-dependent enzyme transketolase from baker's yeast
have been grown from the apo- and the holoform of the enzyme, using PEG as
precipitant. The crystals are orthorhombic, space group P2(1)2(1)2(1) with cell
constants a = 76.3 A, b = 114.2 A, and c = 163.5 A. The crystals are stable in
the x-ray beam and diffract to at least 2.2 A on a conventional x-ray source.
The enzyme is a dimer of identical subunits, and a Vm value of 2.2 A/dalton
indicates that the asymmetric unit contains a dimer. Rotation function
calculations using native data (10-5 A) revealed a local 2-fold rotation axis
with phi = 0 degree and omega = 20 degrees.
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