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