Crystallization and preliminary X-ray analysis of Escherichia coli peptidyl-tRNA hydrolase

Emmanuelle Schmitt; Michel Fromant; Pierre Plateau; Yves Mechulam; Sylvain Blanquet

doi:10.1002/(SICI)1097-0134(199705)28:1<135::AID-PROT14>3.0.CO;2-K

Crystallization and preliminary X-ray analysis of Escherichia coli peptidyl-tRNA hydrolase

Emmanuelle Schmitt
, Michel Fromant
, Pierre Plateau
, Yves Mechulam
, Sylvain Blanquet

Institut Polytechnique de Paris

Résultats de recherche: Contribution à un journal › Article › Revue par des pairs

Résumé

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 P2₁2₁2₁ and diffract to better than 1.2 Å resolution. The structure is being solved by multiple isomorphous replacement.

langue originale	Anglais
Pages (de - à)	135-136
Nombre de pages	2
journal	Proteins: Structure, Function and Genetics
Volume	28
Numéro de publication	1
Les DOIs	https://doi.org/10.1002/(SICI)1097-0134(199705)28:1<135::AID-PROT14>3.0.CO;2-K
état	Publié - 17 mai 1997

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10.1002/(SICI)1097-0134(199705)28:1<135::AID-PROT14>3.0.CO;2-K

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abstract = "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 {\AA}, b = 63.59 {\AA} and c = 62.57 {\AA}. They belong to space group P212121 and diffract to better than 1.2 {\AA} resolution. The structure is being solved by multiple isomorphous replacement.",

keywords = "X-ray structure, crystallization, peptidyl-tRNA hydrolase",

author = "Emmanuelle Schmitt and Michel Fromant and Pierre Plateau and Yves Mechulam and Sylvain Blanquet",

year = "1997",

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T1 - Crystallization and preliminary X-ray analysis of Escherichia coli peptidyl-tRNA hydrolase

AU - Schmitt, Emmanuelle

AU - Fromant, Michel

AU - Plateau, Pierre

AU - Mechulam, Yves

AU - Blanquet, Sylvain

PY - 1997/5/17

Y1 - 1997/5/17

N2 - 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 P212121 and diffract to better than 1.2 Å resolution. The structure is being solved by multiple isomorphous replacement.

AB - 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 P212121 and diffract to better than 1.2 Å resolution. The structure is being solved by multiple isomorphous replacement.

KW - X-ray structure

KW - crystallization

KW - peptidyl-tRNA hydrolase

UR - https://www.scopus.com/pages/publications/0030944952

U2 - 10.1002/(SICI)1097-0134(199705)28:1<135::AID-PROT14>3.0.CO;2-K

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AN - SCOPUS:0030944952

SN - 0887-3585

VL - 28

SP - 135

EP - 136

JO - Proteins: Structure, Function and Genetics

JF - Proteins: Structure, Function and Genetics

IS - 1

ER -

Crystallization and preliminary X-ray analysis of Escherichia coli peptidyl-tRNA hydrolase

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