Crystallization and preliminary X-ray diffraction studies of intact EF-Tu from Thermus aquaticus YT-1.
Many attempts have been made to elucidate the three-dimensional structure from elongation factor Tu, but so far the only crystals suitable for X-ray crystallography contained a partially degraded protein. Here, we report the crystallization of a fully active, intact EF-Tu from thermus aquaticus. The crystals belong to hexagonal space group P6(3)(22) and diffract up to 2.6 A. The cell dimensions are a = b = 178 A, c = 238 A and 6 molecules are contained per asymmetric unit.
D003461:Crystallography; D019204:GTP-Binding Proteins; D008970:Molecular Weight; D010444:Peptide Elongation Factor Tu / Q000302:isolation & purification; D011487:Protein Conformation; D013824:Thermus / Q000201:enzymology*; D014961:X-Ray Diffraction
D019204:GTP-Binding Proteins; D010444:Peptide Elongation Factor Tu