Crystallization and preliminary X-ray analysis of HCE-1, a hatching enzyme of medaka fish, Oryzias latipes

• Published in: Acta crystallographica. Section D, Biological crystallography. Vol. 60; no. 4; pp. 725 - 726
• Main Authors: Kudo, Norio, Yasumasu, Shigeki, Iuchi, Ichiro, Tanokura, Masaru
• Format: Journal Article
• Language: English
• Published: 5 Abbey Square, Chester, Cheshire CH1 2HU, England International Union of Crystallography 01.04.2004
• Subjects: Animals; Cloning, Molecular; Crystallization; Crystallography, X-Ray; hatching enzymes; HCE-1; Metalloendopeptidases - chemistry; Oryzias - embryology; Oryzias - physiology
• ISSN: 1399-0047; 0907-4449; 1399-0047
• DOI: 10.1107/S0907444904001866

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 Å 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 Å, β = 123.6°. The crystal contains one molecule in an asymmetric unit (VM = 2.2 Å3 Da−1) and has a solvent content of 43.7%.