Preliminary crystallographic analysis of a complex between tetracycline and the trypsin-modified form of Escherichia coli elongation factor Tu.
Crystals of a complex between the antibiotic tetracycline and the trypsin-modified form of the Escherichia coli protein elongation factor Tu have been grown in a form suitable for high-resolution X-ray diffraction analysis. The crystals belong to space group P2(1), with cell dimensions a = 69.7 A, b = 156.4 A, c = 135.4 A and beta = 95.3 degrees, and contain six molecules of the complex per asymmetric unit. The crystals are well ordered and diffract to a resolution of 2.3 A.
Mui
S
S
Department of Biochemistry, University of California, Riverside 92521.
Delaria
K
K
Jurnak
F
F
D004926:Escherichia coli; D010444:Peptide Elongation Factor Tu; D013752:Tetracycline; D014357:Trypsin / Q000378:metabolism; D014961:X-Ray Diffraction
D014357:Trypsin; D010444:Peptide Elongation Factor Tu; D013752:Tetracycline