Original Articles
Liang Xu and Zhijun Zhuang
Abstract
100 human genes were study for testing targets for parallel cloning, expression, purification and crystallization. Proteins from these genes had a molecular weight of between 20 and 50 kDa, din not have a high percentage of hydrophobic residues and have unknown crystal structures and were not to be subunits of heterocomplexes. 100 expression clones have been constructed with the GatewayTM cloning system, the results showed that 79 clones were expressed as recombinant proteins in Escherichia coli strain BL21(DE3), 9 clones were expressed as recombinant proteins in Escherichia coli strain Rosetta(DE3), 21 were soluble and 12 have been purified to homogeneity. Crystallization conditions were screened for the purified proteins in 48-well plates by the sitting-drop. After further refinement with the same method or by the hanging-drop method, The crystal of COQ3 were grown