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Crystal structure of (L-Arg)-BO bovine insulin at 0.21 nm resolution

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【作者】 叶升万柱礼刘成国常文瑞梁栋材

【Author】 YE Sheng WAN Zhuli LIU ChengguoCHANG Wenrui ) and LIANG Dongcai(State Key Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences,Beijing 100101, China)

【机构】 State Key Laboratory of BiomacromoleculesInstitute of BiophysicsChinese Academy of SciencesBeijing 100101ChinaChina

【摘要】 <正> The crystal structure of (L-Arg)-B0 bovine insulin has been determined, using data to 0.21 nm and atomic parameters of 2Zn porcine insulin as a starting model, by the difference Fourier method, the restrained least square method and X-PLOR package, interspersed with careful review of the electron density, to a final R-factor of 0.182 and r.m.s. deviation of 0.002 2nm for the bond lengths and 4.3° for the bond angles. The electron densities of additional (L-Arg)-B0 residues to B-chain N-terminus of two monomers in each asymmetric unit are very dear. The crystallographic micro-environment of the N-terminus of the B-chain is different from that of rhombohedral 2-zinc insulin.

【Abstract】 The crystal structure of (L-Arg)-B0 bovine insulin has been determined, using data to 0.21 nm and atomic parameters of 2Zn porcine insulin as a starting model, by the difference Fourier method, the restrained least square method and X-PLOR package, interspersed with careful review of the electron density, to a final R-factor of 0.182 and r.m.s. deviation of 0.002 2nm for the bond lengths and 4.3° for the bond angles. The electron densities of additional (L-Arg)-B0 residues to B-chain N-terminus of two monomers in each asymmetric unit are very dear. The crystallographic micro-environment of the N-terminus of the B-chain is different from that of rhombohedral 2-zinc insulin.

【基金】 Project supported by the Chinese Academy of Sciences and the National Natural Science Foundation of China.
  • 【文献出处】 Science in China(Series C:Life Sciences) ,中国科学(C辑:生命科学)(英文版) , 编辑部邮箱 ,1996年05期
  • 【分类号】Q57
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