1. Crystal Structure Of Human Upstream Binding Factor HMG Domain 5 And Site For The Cell Cycle Regulatory Factor TAF1 Binding 2. Purification, Partial Characterization, Crystallization And Preliminary X-ray Diffraction Of A Novel Cardiotoxin-like Basic Pr

1. Crystal Structure of Human Upstream Binding Factor HMG Domain 5 and Site for the Cell Cycle Regulatory Factor TAF1 BindingThe fifth HMG box domain in human upstream binding factor contributes to rRNA synthesis by RNA polymeraseⅠ(polⅠ). Here, the 2.0 (?) resolution crystal structure of this protein has been solved using single wavelength anomalous dispersion method (SAD). The crystal structure and the reported NMR structure have r.m.s, deviation of 2.18-3.03 (?) for the C~αatoms. However, there are significant differences between the two structures with largest displacement up to 9.0(?). Compared with other HMG boxes structures, the r.m.s, deviations for C~αatoms between hUBF HMG box5 and HMG domains from Drosophila melanogaster protein D and Rattus norvegicus HMG1 are 1.5 and 1.6 (?), respectively. This indicates that the differences between its crystal and NMR structures are larger than its homologous structures. The differences between the two structures reflect potentially its two states with different structures. Moreover, we studied the specific interactions between the hUBF HMG box5 and the first bromodomain in TAF1(TBP-assiociated factor) by ultrasensitive differential scanning calorimetry and chemical shift perturbation. Based on these experimental data, the possible sites in hUBF HMG box5 which may interact with the first bromodomain in TAF1 was proposed.2. Purification, partial characterization, crystallization and preliminary X-ray diffraction of a novel cardiotoxin-like basic protein from Naja naja atra (South Anhui) venomA novel cardiotoxin-like basic protein was isolated from the venom of the Chinese cobra (Naja naja atra) from the south of Anhui in China. The protein inhibits the expression of vascular endothelial growth factor and basic fibroblast growth factor in human lung cancer cell line H1299 and induces the haemolysis of rabbit erythrocytes under low-lecithin conditions. After a two-step chromatographic purification, the resultant 7 kDa protein was crystallized by the hanging-drop vapour-diffusion method at room temperature. A complete data set was collected to 2.35 (?) resolution using an in-house X-ray diffraction system. The crystal belongs to space group P41212, with unit-cell parameters a=b=43.2 (?), c=147.9 (?). There are two molecules in the crystallographic asymmetric unit.