PUBLICATION
Crystallization and preliminary X-ray analysis of ZHE1, a hatching enzyme from the zebrafish Danio rerio
- Authors
- Okada, A., Nagata, K., Sano, K., Yasumasu, S., Kubota, K., Ohtsuka, J., Iuchi, I., and Tanokura, M.
- ID
- ZDB-PUB-091101-6
- Date
- 2009
- Source
- Acta crystallographica. Section F, Structural biology and crystallization communications 65(Pt 10): 1018-1020 (Journal)
- Registered Authors
- Keywords
- ZHE1, hatching enzymes, zebrafish
- MeSH Terms
-
- Animals
- Crystallization
- Crystallography, X-Ray
- Metalloendopeptidases/chemistry*
- Metalloendopeptidases/isolation & purification
- Metalloproteases/chemistry*
- Zebrafish Proteins/chemistry*
- PubMed
- 19851011 Full text @ Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun.
Citation
Okada, A., Nagata, K., Sano, K., Yasumasu, S., Kubota, K., Ohtsuka, J., Iuchi, I., and Tanokura, M. (2009) Crystallization and preliminary X-ray analysis of ZHE1, a hatching enzyme from the zebrafish Danio rerio. Acta crystallographica. Section F, Structural biology and crystallization communications. 65(Pt 10):1018-1020.
Abstract
The hatching enzyme of the zebrafish, ZHE1 (29.3 kDa), is a zinc metalloprotease that catalyzes digestion of the egg envelope (chorion). ZHE1 was heterologously expressed in Escherichia coli, purified and crystallized by the hanging-drop vapour-diffusion method using PEG 3350 as the precipitant. Two diffraction data sets with resolution ranges 50.0-1.80 and 50.0-1.14 A were independently collected from two crystals and were merged to give a highly complete data set over the full resolution range 50.0-1.14 A. The space group was assigned as primitive orthorhombic P2(1)2(1)2(1), with unit-cell parameters a = 32.9, b = 62.5, c = 87.4 A. The crystal contained one ZHE1 molecule in the asymmetric unit.
Genes / Markers
Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Orthology
Engineered Foreign Genes
Mapping