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Updated: Jul 16, 2026

Assessing Two-dimensional Crystallization Trials of Small Membrane Proteins for Structural Biology Studies by Electron Crystallography
Published on: October 30, 2010
Crystals of intact elongation factor Tu from Thermus thermophilus diffracting to high resolution
L S Reshetnikova1, C O Reiser, N K Schirmer
1Laboratorium für Biochemie, Universität Bayreuth, Germany.
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.
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