Crystallization and preliminary X-ray analysis of ZHE1, a hatching enzyme from the zebrafish Danio rerio.
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.
Okada
Akitoshi
A
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.
Nagata
Koji
K
Sano
Kaori
K
Yasumasu
Shigeki
S
Kubota
Keiko
K
Ohtsuka
Jun
J
Iuchi
Ichiro
I
Tanokura
Masaru
M
D000818:Animals; D003460:Crystallization; D018360:Crystallography, X-Ray; D008666:Metalloendopeptidases / Q000737:chemistry* / Q000302:isolation & purification; D045726:Metalloproteases / Q000737:chemistry*; D029961:Zebrafish Proteins / Q000737:chemistry*
D029961:Zebrafish Proteins; D045726:Metalloproteases; C546730:he1.2 protein, zebrafish; D008666:Metalloendopeptidases; C024344:envelysin