CRYSTALLIZATION OF GREA, A TRANSCRIPT CLEAVAGE FACTOR FROM ESCHERICHIA-COLI

GreA is a 17.6 kDa protein from Escherichia coli that induces cleavage of the nascent transcript in the elongating complex of RNA polymerase , followed by release of the 3'-terminal fragment. Crystals of GreA ha ve been obtained form polyethylene glycol 4000, 2-propanol and sodium citrate, pH 5.6 and have been propogated by a novel seeding procedure. The crystals diffract beyond 2 Angstrom resolution and belong to the orthorhombic space group P2(1)2(1)2(1), with cell dimensions a = 101.7 Angstrom, b = 42.22 Angstrom, c = 40.05 Angstrom and with one molecul e in the asymmetric unit.