CRYSTALLIZATION AND PRELIMINARY-X-RAY DIFFRACTION STUDIES OF PANCREATIC SPASMOLYTIC POLYPEPTIDE

被引：8

作者：

GORMAN, MA

DE, A

FREEMONT, PS

机构：

[1] Protein Structure Laboratory, Imperial Cancer Research Fund 44 Lincoln's Inn Fields, London

来源：

JOURNAL OF MOLECULAR BIOLOGY | 1992年 / 228卷 / 03期

关键词：

CRYSTALLIZATION; PANCREATIC SPASMOLYTIC POLYPEPTIDE; X-RAY CRYSTALLOGRAPHY; ROTATION FUNCTION;

D O I：

10.1016/0022-2836(92)90884-M

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Pancreatic spasmolytic polypeptide (PSP) isolated from porcine pancreas has been crystallized by the hanging drop vapour diffusion method. The crystals belong to the space group I222 or I212121 with cell dimensions a = 181·9 A ̊, b = 54·5 A ̊, c = 72·9 A ̊. The crystals diffract to at least 2·5 Å resolution and the asymmetric unit contains two molecules (Vm = 3·9 A ̊3/Da) with a solvent content of 68% as determined by density measurements of the crystals. The self-rotation function suggests that the two molecules within the asymmetric unit are related by a 2-fold axis at either 30 ° or 60 ° from a in a plane perpendicular to the b axis. © 1992.

引用

页码：991 / 994

页数：4

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