J Mol Biol. 1992 Dec 5;228(3):991-4.

Crystallization and preliminary X-ray diffraction studies of pancreatic spasmolytic polypeptide.

Source

Protein Structure Laboratory, Imperial Cancer Research Fund, London, England.

Abstract

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 I2(1)2(1)2(1) with cell dimensions a = 181.9 A, b = 54.5 A, c = 72.9 A. The crystals diffract to at least 2.5 A resolution and the asymmetric unit contains two molecules (Vm = 3.9 A3/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 degrees or 60 degrees from a in a plane perpendicular to the b axis.

PMID:: 1469732; [PubMed - indexed for MEDLINE]

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Cited by 1 PubMed Central article

Crystal structure of a disulfide-linked "trefoil" motif found in a large family of putative growth factors. [Proc Natl Acad Sci U S A. 1994]
Crystal structure of a disulfide-linked "trefoil" motif found in a large family of putative growth factors.
De A, Brown DG, Gorman MA, Carr M, Sanderson MR, Freemont PS. Proc Natl Acad Sci U S A. 1994 Feb 1; 91(3):1084-8.

Structures reported by this article

Crystal Structure Of A Novel Disulfide-Linked "trefoil" Motif Found In A Large Family Of Putative Growth Factors

PDB: 1POS

Source: Sus scrofa

Method: X-Ray Diffraction

Resolution: 2.6 Å

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