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Crystallization and preliminary X‐ray crystallographic analysis of ImmE7 protein of colicin E7
Author(s) -
Ku WenYen,
Wang ChingShao,
Chen ChiehYen,
Chak KinFu,
Safo Martin K.,
Yuan Hanna S.
Publication year - 1995
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.340230414
Subject(s) - orthorhombic crystal system , colicin , monoclinic crystal system , crystallography , crystallization , resolution (logic) , chemistry , x ray , crystal structure , physics , escherichia coli , biochemistry , optics , organic chemistry , artificial intelligence , computer science , gene
The ImmE7 protein, which can bind specifically to the DNase colicin E7 and neutralize its bactericidal activity, has been purified and crystallized in two different crystal forms by vapor diffusion method. The orthorhombic crystals belong to space group I 222 or I 2 1 2 1 2 1 and have unit cell dimensions a = 75.1 Å, b = 50.5 Å, and c = 45.4 Å. The second form is monoclinic space group P 2 1 with ceil dimensions a = 29.3 Å, b = 102.7 Å, c = 53.0 Å and β = 91.5°. The orthorhombic crystals diffract to 1.8 Å resolution, and are suitable for high‐resolution X‐ray analysis. © 1995 Wiley‐Liss, Inc.