Crystallization and preliminary X-ray analysis of porcine ribonuclease inhibitor, a protein with leucine-rich repeats.
Ribonuclease inhibitor was purified from pig liver and crystallized at 21 degrees C from solutions containing dithiothreitol as an additive and ammonium sulfate, lithium sulfate or combinations of both as precipitants. Crystals have the symmetry of the tetragonal space group I4 with a = 134.9 A and c = 83.6 A, and diffract to better than 3 A resolution. Self rotation functions and packing density of the crystals are consistent with two molecules in the asymmetric unit.
Howard Hughes Medical Institute, University of Texas Southwestern Medical Center, Dallas 75235-9050.
B
B
Kobe
J
J
Deisenhofer
D000818:Animals; D003460:Crystallization; D047908:Intracellular Signaling Peptides and Proteins; D007930:Leucine; D008099:Liver / Q000378:metabolism; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry* / Q000302:isolation & purification; D012260:Ribonucleases / Q000037:antagonists & inhibitors; D013552:Swine; D014961:X-Ray Diffraction
D047908:Intracellular Signaling Peptides and Proteins; D011506:Proteins; C066953:ribonuclease inhibitor, porcine; D012260:Ribonucleases; D007930:Leucine