title: Crystallization and preliminary X-ray diffraction studies of aspartic proteinase from Irpex lacteus.
abstract: Crystals of ILAP (Irpex lacteus aspartic proteinase) have been obtained by the hanging drop method using ammonium sulfate as a precipitant. The crystals are monoclinic, space group P2(1) with cell dimensions a = 54.5 A, b = 79.6 A, c = 37.5 A, beta = 96.8 degrees. The crystals are quite stable to X-rays and diffract beyond 1.9 A resolution. There is one molecule in the asymmetric unit.
authors.affiliation: Biological Function Division, National Food Research Institute, Ibaraki, Japan.
authors.forename: H
authors.initials: H
authors.lastname: Kobayashi
authors.forename: K
authors.initials: K
authors.lastname: Kasamo
authors.forename: H
authors.initials: H
authors.lastname: Mizuno
authors.forename: H
authors.initials: H
authors.lastname: Kim
authors.forename: I
authors.initials: I
authors.lastname: Kusakabe
authors.forename: K
authors.initials: K
authors.lastname: Murakami
mesh_terms: D000818:Animals; D016282:Aspartic Acid Endopeptidases / Q000737:chemistry*; D001487:Basidiomycota / Q000201:enzymology*; D003460:Crystallization; D012689:Sequence Homology, Nucleic Acid; D014961:X-Ray Diffraction
chemical_list: D016282:Aspartic Acid Endopeptidases; C076494:aspartic proteinase, Irpex lacteus