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Crystallization and preliminary x‐ray analysis of Escherichia coli peptidyl‐tRNA hydrolase
Author(s) -
Schmitt Emmanuelle,
Fromant Michel,
Plateau Pierre,
Mechulam Yves,
Blanquet Sylvain
Publication year - 1997
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/(sici)1097-0134(199705)28:1<135::aid-prot14>3.0.co;2-k
Subject(s) - orthorhombic crystal system , escherichia coli , polyethylene glycol , crystallization , hydrolase , transfer rna , resolution (logic) , monomer , chemistry , molecular replacement , crystallography , gene , crystal structure , biochemistry , enzyme , rna , polymer , organic chemistry , artificial intelligence , computer science
Peptidyl‐tRNA hydrolase from Escherichia coli, a monomer of 21 kDa, was overexpressed from its cloned gene pth and crystallized by using polyethylene glycol as precipitant. The crystals are orthorhombic and have unit cell parameters a = 47.24 Å, b = 63.59 Å, and c = 62.57 Å. They belong to space group P2 1 2 1 2 1 and diffract to better than 1.2 Å resolution. The structure is being solved by multiple isomorphous replacement. © 1997 Wiley‐Liss Inc.