CRYSTALLIZATION OF A NOVEL ESTERASE WHICH INACTIVATES THE MACROLIDE TOXIN BREFELDIN-A

A novel esterase obtained from Bacillus subtilis and capable of hydrol yzing the phytotoxin brefeldin A was crystallized using the hanging-dr op technique. The crystals have two forms and both are monoclinic: for m I, space group P2(1) with a = 101.7. b = 64.1, c = 55.4 Angstrom and B = 102.5 degrees, and form II, space group C2. with a = 140.7, b = 8 2.6, c = 81.5 Angstrom and beta = 112.5 degrees. There are two molecul es related by a pronounced non-crystallographic dyad per asymmetric un it in both crystal forms. The crystals diffract to 2.3 Angstrom using a rotating-anode X-ray source.