MOLECULAR-STRUCTURE OF A DIMER COMPOSED OF VARIABLE PORTIONS OF BENCE-JONES PROTEIN REI REFINED AT 2.0-A RESOLUTION
MOLECULAR-STRUCTURE OF A DIMER COMPOSED OF VARIABLE PORTIONS OF BENCE-JONES PROTEIN REI REFINED AT 2.0-A RESOLUTION
复制标题
DOI：
10.1021/bi00693a025
复制
发表时间：
1975-01-01
期刊：
影响因子：
2.9
通讯作者：
PALM, W
中科院分区：
文献类型：
--
作者：
EPP, O;LATTMAN, EE;PALM, W
Otto Epp，* Eaton E. Lattman，* 1 Marianne Schiffer J Robert Huber，and Walter Palm #摘要：a型Bence-Jones蛋白REI形成二聚体的可变部分的结构已通过X射线衍射确定，分辨率为2.0 nm。该结构已被细化使用约束晶体学细化程序。对于15，000个显著测量的反射，最终R值为0.24;原子位置的估计标准偏差为0.09 μ m。通过比较两种独立精制的单体，可以更客观地评估原子位置的误差。内链段中两条链的主链原子平均偏差为0.22 π，主链间夹角为6.3。Vrei二聚体的未精制分子结构已经公开（Epp，O.，Colman，P.，Fehlhammer，H.，Bode，W.，Schiffer，M.，胡贝尔河，和Palm，W.（1974），Eur. 45，513）。现从氢键和构象角度进行详细分析。二级结构
Otto Epp,* Eaton E. Lattman,* 1 Marianne SchifferJ Robert Huber, and Walter Palm# abstract: The structure of the variable portions of a-type Bence-Jones protein REI forming a dimer has been determined by X-ray diffraction to a resolution of 2.0 Á. The structure has been refined using a constrained crystallographic refinement procedure. The final R value is 0.24 for 15,000 significantly measured reflections; the estimated standard deviation of atomic positions is 0.09 Á. A more objective assessment of the error in the atomic positions is possible by comparing the two independently refined mono-mers. The mean deviation of main-chain atoms of the two chains in internal segments is 0.22 Á, of main-chaindihe-dral angles 6.3 for these segments. The unrefined molecular structure of the Vrei dimer has been published (Epp, O., Colman, P., Fehlhammer, H., Bode, W., Schiffer, M., Huber, R., and Palm, W.(1974), Eur. J. Biochem. 45, 513). Now a detailed analysis is presented in terms of hy-drogen bonds and conformational angles. Secondary struc-