title: Crystallization and preliminary X-ray analysis of HCE-1, a hatching enzyme of medaka fish, Oryzias latipes.
abstract: The hatching enzyme of medaka fish, high choriolytic enzyme (HCE-1; MW = 22.7 kDa), was crystallized by the hanging-drop vapour-diffusion method using PEG 10 000 as the precipitant. The hatching enzyme is a metalloproteinase which is secreted from the embryo at the time of hatching. The crystals diffracted X-rays to beyond 1.34 A resolution using a synchrotron-radiation source. The crystals belonged to the monoclinic space group C2, with unit-cell parameters a = 99.0, b = 30.4, c = 79.6 A, beta = 123.6 degrees. The crystal contains one molecule in an asymmetric unit (VM = 2.2 A3 Da-1) and has a solvent content of 43.7%.
authors.affiliation: Department of Applied Biological Chemistry, Graduate School of Agricultural and Life Sciences, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-8657, Japan.
authors.forename: Norio
authors.initials: N
authors.lastname: Kudo
authors.forename: Shigeki
authors.initials: S
authors.lastname: Yasumasu
authors.forename: Ichiro
authors.initials: I
authors.lastname: Iuchi
authors.forename: Masaru
authors.initials: M
authors.lastname: Tanokura
mesh_terms: D000818:Animals; D003001:Cloning, Molecular; D003460:Crystallization; D018360:Crystallography, X-Ray; D008666:Metalloendopeptidases / Q000737:chemistry*; D009990:Oryzias / Q000196:embryology / Q000502:physiology*
chemical_list: D008666:Metalloendopeptidases; C024344:envelysin