CRYSTALLIZATION AND PRELIMINARY-X-RAY ANALYSIS OF THE 2 DOMAINS OF GLUCOSAMINE-6-PHOSPHATE SYNTHASE FROM ESCHERICHIA-COLI

The glutamine amidohydrolase and fructose 6-phosphate binding domains of glucosamine-6-phosphate synthase from Escherichia coli have been ov erexpressed, purified and crystallized for X-ray diffraction analysis. The crystals of the glutamine amidohydrolase domain belong to the ort horhombic space group P2(1)2(1)2(1) with cell dimensions a = 70.4 Angs trom, b = 82.5 Angstrom, c = 86.1 Angstrom, with two molecules in the asymmetric unit, and diffract to 1.9 Angstrom resolution. The native P atterson indicated pseudo c-face centering of the unit cell. The fruct ose 6-phosphate binding domain was crystallized in the hexagonal space group P6(1) or P6(5) with cell dimensions a = b = 63.5 Angstrom, c = 334.3 Angstrom and with two molecules in the asymmetric unit. Diffract ion data to 2.6 Angstrom resolution have been collected.