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【期刊论文】Crystal Structure of Hemolin: A Horseshoe Shape with Implications for Homophilic Adhesion
苏晓东, Xiao-Dong Su, * Louis N. Gastinel, † Daniel E. Vaughn, ‡ Ingrid Faye, Pak Poon, Pamela J. Bjorkman §
SCIENCE VOL 281 14 AUGUST 1998,-0001,():
-1年11月30日
Hemolin, an insect immunoglobulin superfamily member, is a lipopolysaccharide-binding immune protein induced during bacterial infection. The 3.1 angstrom crystal structure reveals a bound phosphate and patches of positive charge, which may represent the lipopolysaccharide binding site, and a new and unexpected arrangement of four immunoglobulin-like domains forming a horseshoe. Sequence analysis and analytical ultracentrifugation suggest that the domain arrangement is a feature of the L1 family of neural cell adhesion molecules related to hemolin. These results are relevant to interpretation of human L1 mutations in neurological diseases and suggest a domain swapping model for how L1 family proteins mediate homophilic adhesion.
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苏晓东, Shahrzad Bakhtiar, a Jitka VeÂvodovaÂ, b† Rajni Hatti-Kaul a and Xiao-Dong Sub *
Acta Cryst. (2003). D59, 529-531,-0001,():
-1年11月30日
A novel calcium-independent serine protease from an alkaliphilic bacterium, Nesterenkonia sp. AL20, has been purified and crystallized at 296 Kusing sodium formate as the main precipitant. This enzyme is optimally active at pH 10, exhibits high stability towards autolytic digestion and its stability is not affected by the presence of EDTA or detergents. The triangular prism-shaped crystals diffracted X-rays to beyond 1.5 A
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【期刊论文】Structural genomics efforts at the Chinese Academy of Sciences and Peking University
苏晓东, W.M. Gong, H.Y. Liu, L.W. Niu, Y.Y. Shi, *, Y.J. Tang, M.K. Teng, J.H. Wu, D.C. Liang, D.C. Wang, J.F. Wang, J.P. Ding, H.Y. Hu, Q.H. Huang, Q.H. Zhang, S.Y. Lu, J.L. An, Y.H. Liang, X.F. Zheng, X.C. Gu & X.D. Su
Journal of Structural and Functional Genomics 4: 137-139, 2003.,-0001,():
-1年11月30日
Structural genomics efforts at the Chinese Academy of Sciences and Peking University are reported in this article. The major targets for the structural genomics project are targeted proteins expressed in human hematopoietic stem/progenitor cells, proteins related to blood diseases and other human proteins. Up to now 328 target genes have been constructed in expression vectors. Among them, more than 50% genes have been expressed in Escherichia coli, approximately 25% of the resulting proteins are soluble, and 35 proteins have been purified. Crystallization, data collection and structure determination are continuing. Experiences accumulated during this initial stage are useful for designing and applying high-throughput approaches in structural genomics.
blood disease,, hematopoietic stem/, progenitor cells,, nuclear magnetic resonance,, protein structure,, structural genomics,, X-ray rystallography
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苏晓东
,-0001,():
-1年11月30日
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苏晓东, Hui Ren, a, Yuhe Liang, b, Rui Li, Haitao Ding a, Shihong Qiu, c, Shanyun Lua, Jianli An a, Lanfen Li a, Ming Luo, c Xiaofeng Zheng a, * and Xiao-Dong Sua
Acta Cryst. (2004). D60, 1292-1294,-0001,():
-1年11月30日
The adrenal gland protein AD-004 was identified in the human adrenal gland. Full-length AD-004 contains 172 amino acids, with a predicted molecular weight of about 20kDa. In attempts to crystallize human AD-004, the gene was subcloned into a modified pET vector, pET21-DEST, with an N-terminal His5 tag using the Gateway cloning system, followed by protein expression in Escherichia coli strain BL21(DE3). The protein was purified in two steps to near-homogeneity and was crystallized. The crystals belong to space group P61 or P65, with unit-cell parameters a= b=99.56, c= 57.19 A
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