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.
Schneider
G
G
Department of Molecular Biology, Swedish University of Agricultural Sciences, Uppsala Biomedical Centre.
Sundström
M
M
Lindqvist
Y
Y
D003460:Crystallization; D011487:Protein Conformation; D012441:Saccharomyces cerevisiae / Q000201:enzymology*; D014174:Transketolase / Q000302:isolation & purification; D014961:X-Ray Diffraction
D014174:Transketolase