Arnold E, Rossmann M G
Department of Biological Sciences, Purdue University, West Lafayette, Indiania 47907.
Acta Crystallogr A. 1988 May 1;44 ( Pt 3):270-82. doi: 10.1107/s0108767387011875.
The structure of human rhinovirus 14 has been refined, by the method of restrained least squares, to an R factor of 0.16 for various random samples between 6 and 3 A resolution with F greater than 3 sigma (F). As a first step the non-crystallographic symmetry parameters were optimized using the initial atomic model in a rigid-body refinement procedure. Phase determination by the molecular-replacement phase extension and refinement procedure was continued to 2.94 A resolution, employing the improved non-crystallographic symmetry operators. The resultant structure-factor phases and weights, together with the measured amplitudes, constituted the X-ray observations used in the restrained refinement. The Hendrickson-Konnert program system [Konnert & Hendrickson (1980). Acta Cryst. A36, 344-350] was modified to incorporate non-crystallographic symmetry constrains and structure-factor phases as observations. The non-bonded contacts between subunits related by non-crystallographic symmetry were also restrained.
人类鼻病毒14的结构已通过约束最小二乘法进行了优化，对于6至3埃分辨率之间的各种随机样本，R因子为0.16，F大于3σ（F）。作为第一步，在刚体优化过程中使用初始原子模型优化非晶体学对称参数。通过分子置换相扩展和优化程序进行的相位确定持续到2.94埃分辨率，采用改进的非晶体学对称算子。所得的结构因子相位和权重，连同测量的振幅，构成了约束优化中使用的X射线观测数据。对Hendrickson-Konnert程序系统[Konnert & Hendrickson (1980). Acta Cryst. A36, 344 - 350]进行了修改，以纳入非晶体学对称约束和作为观测数据的结构因子相位。由非晶体学对称相关的亚基之间的非键接触也受到约束。
