Crystals of intact elongation factor Tu from Thermus thermophilus diffracting to high resolution.
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.
Reshetnikova
L S
LS
Laboratorium für Biochemie, Universität Bayreuth, Germany.
Reiser
C O
CO
Schirmer
N K
NK
Berchtold
H
H
Storm
R
R
Hilgenfeld
R
R
Sprinzl
M
M
D003460:Crystallization; D004591:Electrophoresis, Polyacrylamide Gel; D010444:Peptide Elongation Factor Tu / Q000737:chemistry*; D016963:Thermus thermophilus / Q000737:chemistry*; D014961:X-Ray Diffraction
D010444:Peptide Elongation Factor Tu