Fedorov A A, Chernaia M M, Strokopytov B V, Nikitenko A V, Fonarev Iu D, Kuzin A P
Bioorg Khim. 1993 Jan;19(1):33-42.
The human progastricsin crystal structure has been solved by the molecular replacement method. The intensities of reflections from native progastricsin crystals were measured at the 4.0 A resolution by the omega-scan method with a Nicolet P3 diffractometer operated in automatic regime. To determine the orientation and position of progastricsin molecules in the unit cell, programme packages MERLOT and BRUTE were applied running on a MicroVAX-II computer. Prior to the translation search, several rotation function peaks were subjected to a rigid body refinement against the correlation coefficient between the observed and calculated structure factors. This approach clearly identified the correct orientation of the molecule. The solution obtained from the BRUTE translation function map was refined by the 6-dimensional correlation search and then by programme CORELS. The human progastricsin molecules packing in the crystal unit ell is described.
人胃蛋白酶原晶体结构已通过分子置换法解析。用自动运行的Nicolet P3衍射仪，采用ω扫描法在4.0 Å分辨率下测量天然胃蛋白酶原晶体的衍射强度。为了确定胃蛋白酶原分子在晶胞中的取向和位置，在MicroVAX-II计算机上运行MERLOT和BRUTE程序包。在进行平移搜索之前，针对观测和计算结构因子之间的相关系数，对几个旋转函数峰进行刚体精修。这种方法明确地确定了分子的正确取向。从BRUTE平移函数图获得的解通过六维相关搜索，然后通过CORELS程序进行精修。描述了晶体单位晶胞中人类胃蛋白酶原分子的堆积情况。
