Crystallization and preliminary X-ray crystallographic analysis of the cysteine protease inhibitor clitocypin.
Clitocypin is a cysteine protease inhibitor from the mushroom Clitocybe nebularis. The protein has been purified from natural sources and crystallized in a variety of non-isomorphous forms belonging to monoclinic and triclinic space groups. A diffraction data set to 1.55 A resolution was obtained from a crystal belonging to space group P2, with unit-cell parameters a = 38.326, b = 33.597, c = 55.568 A, beta = 104 degrees. An inability to achieve isomorphism forced the use of MAD and SAD phasing methods. Phasing is in progress.
Galesa
Katja
K
Department of Biochemistry and Molecular Biology, JoZef Stefan Institute, Jamova 39, 1000 Ljubljana, Slovenia.
Brzin
Joze
J
Sabotic
Jerica
J
Turk
Dusan
D
D000363:Agaricales / Q000201:enzymology*; D018360:Crystallography, X-Ray; D015853:Cysteine Proteinase Inhibitors / Q000737:chemistry* / Q000302:isolation & purification; D005656:Fungal Proteins / Q000737:chemistry* / Q000302:isolation & purification
C411656:Clitocypin protein, Clitocybe nebularis; D015853:Cysteine Proteinase Inhibitors; D005656:Fungal Proteins