Crystals of intact elongation factor Tu from Thermus thermophilus diffracting to high resolution

L S Reshetnikova; C O Reiser; N K Schirmer; H Berchtold; R Storm; R Hilgenfeld; M Sprinzl

doi:10.1016/0022-2836(91)80058-3

Crystals of intact elongation factor Tu from Thermus thermophilus diffracting to high resolution

J Mol Biol. 1991 Sep 20;221(2):375-7. doi: 10.1016/0022-2836(91)80058-3.

Authors

L S Reshetnikova¹, C O Reiser, N K Schirmer, H Berchtold, R Storm, R Hilgenfeld, M Sprinzl

Affiliation

¹ Laboratorium für Biochemie, Universität Bayreuth, Germany.

PMID: 1920424
DOI: 10.1016/0022-2836(91)80058-3

Abstract

The intact elongation factor Tu from the extreme thermophile Thermus thermophilus has been crystallized as a complex with the GTP analogue guanosine-5'-(beta,gamma-imido)triphosphate. The crystals are very stable in the X-ray beam and diffract to 1.9 A resolution. They exhibit space group C2, with a = 150.3(6) A, b = 99.6(3) A, c = 40.1(1) A, beta = 95.4(2) degrees, and contain one elongation factor Tu molecule per asymmetric unit.

Publication types

Review

MeSH terms

Crystallization
Electrophoresis, Polyacrylamide Gel
Peptide Elongation Factor Tu / chemistry*
Thermus thermophilus / chemistry*
X-Ray Diffraction

Substances

Peptide Elongation Factor Tu