Crystallization and preliminary x-ray crystallographic study of NADH-cytochrome b5 reductase from pig liver microsomes.
Crystals of the hydrophilic, catalytic domain (30 kDa) of pig liver NADH-cytochrome b5 reductase solubilized by the protease (cathepsin D) have been grown in a solution of polyethylene glycol by the vapor-diffusion procedure. The crystals belong to the orthorhombic system, space group P2(1)2(1)2(1) with unit-cell dimensions of a = 87.1, b = 73.2, and c = 49.0 A. The asymmetric unit contains one molecule of the enzyme. The x-ray diffraction patterns extend to 2.0-A resolution. On the other hand, the intact enzyme (35 kDa) containing the hydrophobic membrane-binding domain solubilized by the detergent (Triton N-101) has been crystallized also from the polyethylene glycol solution. The crystals are needle-shaped and still too small for x-ray diffraction study.
D000818:Animals; D002402:Cathepsin D / Q000378:metabolism; D003460:Crystallization; D003579:Cytochrome Reductases; D042966:Cytochrome-B(5) Reductase; D008862:Microsomes, Liver / Q000201:enzymology*; D013552:Swine; D014961:X-Ray Diffraction
D003579:Cytochrome Reductases; D042966:Cytochrome-B(5) Reductase; D002402:Cathepsin D