Crystallization and preliminary X-ray analysis of ZHE1, a hatching enzyme from the zebrafish Danio rerio
Crystallization and preliminary X-ray analysis of ZHE1, a hatching enzyme from the zebrafish Danio rerio
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DOI：
10.1107/s1744309109033016
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发表时间：
2009-10-01
影响因子：
0.9
通讯作者：
Tanokura, Masaru
中科院分区：
文献类型：
--
作者：
Okada, Akitoshi;Nagata, Koji;Tanokura, Masaru
斑马鱼的孵化酶ZHE 1（29.3 kDa）是一种锌金属蛋白酶，催化卵包膜（绒毛膜）的消化。ZHE 1在大肠杆菌中异源表达，用PEG 3350作为沉淀剂，通过悬滴气相扩散法进行纯化和结晶。从两个晶体中独立地收集分辨率范围为50.0-1.80和50.0-1.14埃的两个衍射数据集，并将其合并以给出在整个分辨率范围50.0-1.14埃上的高度完整的数据集。空间群为原始正交晶系P2（1）2（1）2（1），晶胞参数a = 32.9，B = 62.5，c = 87.4埃。该晶体在不对称单元中含有一个ZHE 1分子。
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 angstrom 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 angstrom. 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 angstrom. The crystal contained one ZHE1 molecule in the asymmetric unit.