Crystallization and preliminary X-ray analysis of HCE-1, a hatching enzyme of medaka fish, Oryzias latipes
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 di...
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Published in | Acta crystallographica. Section D, Biological crystallography. Vol. 60; no. 4; pp. 725 - 726 |
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Main Authors | , , , |
Format | Journal Article |
Language | English |
Published |
5 Abbey Square, Chester, Cheshire CH1 2HU, England
International Union of Crystallography
01.04.2004
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Subjects | |
Online Access | Get full text |
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Summary: | 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%. |
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Bibliography: | ArticleID:AYDPU5038 ark:/67375/WNG-KWR7D050-K istex:6118B6C924B169884AB540DF2CCD35D23DA806BF ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 1399-0047 0907-4449 1399-0047 |
DOI: | 10.1107/S0907444904001866 |