title: Crystallization and preliminary X-ray study of horse pancreatic lipase.
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.
authors.affiliation: Centre de Biochimie et de Biologie Moléculaire C.N.R.S., Marseille, France.
authors.forename: D
authors.initials: D
authors.lastname: Lombardo
authors.forename: C
authors.initials: C
authors.lastname: Chapus
authors.forename: Y
authors.initials: Y
authors.lastname: Bourne
authors.forename: C
authors.initials: C
authors.lastname: Cambillau
mesh_terms: D000818:Animals; D003460:Crystallization; D006736:Horses; D008049:Lipase / Q000302:isolation & purification; D010179:Pancreas / Q000201:enzymology*; D014961:X-Ray Diffraction
chemical_list: D008049:Lipase