Title : Crystallization and preliminary X-ray study of horse pancreatic lipase - Lombardo_1989_J.Mol.Biol_205_259 |
Author(s) : Lombardo D , Chapus C , Bourne Y , Cambillau C |
Ref : Journal of Molecular Biology , 205 :259 , 1989 |
Abstract :
Horse (Equus caballus) pancreatic lipase (EC 3.1.1.3) has been crystallized using the hanging drop method of vapour diffusion at 20 degrees C. The best crystals were grown from an 8 mg/ml solution in 10 to 20% (w/v) polyethylene glycol 8000, 10 mM-MgCl2, 0.1 M-NaCl, 0.1 M-Mes buffer (pH 5.6). They reach dimensions of 0.8 mm x 0.4 mm x 0.6 mm. X-ray examination of the lipase crystals shows that they are orthorombic with a space group P2(1)2(1)2(1). Their cell dimensions are a = 79.8 A, b = 97.2 A c = 145.3 A. Two molecules per asymmetric unit give a Vm value of 2.82 A3/dalton (56% water content). Lipase crystals strongly diffract to at least 1.8 A resolution. Some molecular properties of horse lipase compared to those of the better-known porcine enzyme are also presented. |
PubMedSearch : Lombardo_1989_J.Mol.Biol_205_259 |
PubMedID: 2926806 |
Gene_locus related to this paper: horse-1plip |
Gene_locus | horse-1plip |
Lombardo D, Chapus C, Bourne Y, Cambillau C (1989)
Crystallization and preliminary X-ray study of horse pancreatic lipase
Journal of Molecular Biology
205 :259
Lombardo D, Chapus C, Bourne Y, Cambillau C (1989)
Journal of Molecular Biology
205 :259