Crystallization and preliminary X-ray diffraction studies of pancreatic spasmolytic polypeptide.
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.
Gorman
M A
MA
Protein Structure Laboratory, Imperial Cancer Research Fund, London, England.
De
A
A
Freemont
P S
PS
D000818:Animals; D003460:Crystallization; D036341:Intercellular Signaling Peptides and Proteins; D009077:Mucins; D009124:Muscle Proteins; D009479:Neuropeptides; D010179:Pancreas / Q000737:chemistry*; D010276:Parasympatholytics / Q000737:chemistry*; D010455:Peptides / Q000737:chemistry*; D013552:Swine; D000071164:Trefoil Factor-2; D000071165:Trefoil Factor-3; D014961:X-Ray Diffraction
D036341:Intercellular Signaling Peptides and Proteins; D009077:Mucins; D009124:Muscle Proteins; D009479:Neuropeptides; D010276:Parasympatholytics; D010455:Peptides; C099037:TFF3 protein, rat; C000604008:Tff2 protein, rat; D000071164:Trefoil Factor-2; D000071165:Trefoil Factor-3; C034407:pancreatic spasmolytic polypeptide