Crystallization and preliminary X-ray diffraction studies of aspartic proteinase from Irpex lacteus.
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.
Kobayashi
H
H
Biological Function Division, National Food Research Institute, Ibaraki, Japan.
Kasamo
K
K
Mizuno
H
H
Kim
H
H
Kusakabe
I
I
Murakami
K
K
D000818:Animals; D016282:Aspartic Acid Endopeptidases / Q000737:chemistry*; D001487:Basidiomycota / Q000201:enzymology*; D003460:Crystallization; D012689:Sequence Homology, Nucleic Acid; D014961:X-Ray Diffraction
D016282:Aspartic Acid Endopeptidases; C076494:aspartic proteinase, Irpex lacteus