Preliminary crystallographic data for transketolase from yeast.


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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@article{Schneider1989PreliminaryCD, title={Preliminary crystallographic data for transketolase from yeast.}, author={G{\"{u}nter Schneider and Manya Sundstr{\"{o}m and Ylva Lindqvist}, journal={The Journal of biological chemistry}, year={1989}, volume={264 36}, pages={21619-20} }