Crystals of threonyl-tRNA synthetase from Thermus thermophilus. Preliminary crystallographic data.

Journal of molecular biology ·Vol. 214 ·No. 4 ·1990-08-20 ·Pages 819-20

Garber MB, Yaremchuk AD, Tukalo MA, Egorova SP, Fomenkova NP, Nikonov SV

Abstract

Crystals have been obtained of threonyl-tRNA synthetase from the extreme thermophile Thermus thermophilus using sodium formate as a precipitant. The crystals are very stable and diffract to at least 2.4 A. The crystals belong to space group P2(1)2(1)2(1) with cell parameters a = 61.4 A, b = 156.1 A, c = 177.3 A.

MeSH Terms

Amino Acyl-tRNA Synthetases/isolation & purification Crystallization Enzyme Stability Protein Conformation Thermus/enzymology Threonine-tRNA Ligase/isolation & purification X-Ray Diffraction

Chemicals

Amino Acyl-tRNA Synthetases Threonine-tRNA Ligase

Authors & Affiliations

6 authors, click to expand affiliations / ORCID

Garber M B

Institute of Protein Research, Academy of Sciences of the U.S.S.R., Puschino, Moscow Region.

Yaremchuk A D

Tukalo M A

Egorova S P

Fomenkova N P

Nikonov S V

Article Info

Journal

Journal of molecular biology

Abbr.

J Mol Biol

ISSN

0022-2836

DOI

10.1016/0022-2836(90)90337-L

Published

1990-08-20

Pages

819-20

Language

English

Region

England

NLM ID

2985088R

Subset

External Links

PubMed source DOI: 10.1016/0022-2836(90)90337-L View journal details

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Crystals of threonyl-tRNA synthetase from Thermus thermophilus. Preliminary crystallographic data.

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