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Updated: Jun 22, 2026
Chromatographic Purification of Highly Active Yeast Ribosomes
Published on: October 24, 2011
Cloning, purification, crystallization and preliminary crystallographic analysis of a ribokinase from Staphylococcus
Lin Wang1, Haipeng Wang, Jianbin Ruan
1School of Life Sciences, University of Science and Technology of China, 96 Jinzhai Road, Hefei, Anhui 230027, People's Republic of China.
Abstract:
The gene SA239 from Staphylococcus aureus encodes a ribokinase that catalyzes the phosphorylation of D-ribose to produce ribose-5-phosphate. Sa239 was crystallized using the hanging-drop vapour-diffusion method. The crystals diffracted to 2.9 A resolution and belonged to space group P6(1)22 or P6(5)22, with unit-cell parameters a = b = 91.8, c = 160.7 A. Preliminary crystallographic analysis revealed that the Matthews coefficient V(M) was 3.01 A(3) Da(-1), indicating the presence of one molecule in the asymmetric unit.
