Preliminary x-ray diffraction data for tetragonal crystals of trypsinized Escherichia coli elongation factor.

Abstract Trypsin-cleaved elongation factor EF-Tu-GDP from Escherichia coli crystallizes in several different unit cells. The optimal crystal form for high resolution X-ray diffraction studies belongs to space group P 4 1 2 1 2 with a = 70.4 A and c = 161.4 A . There is one polypeptide chain ( M r = 36,000) per asymmetric unit. The tetragonal crystals are well-ordered, stable under X-ray exposure and diffract to at least 2.3 A resolution.