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  • Title: Crystallization of a novel esterase which inactivates the macrolide toxin brefeldin A.
    Author: Wei Y, Swenson L, Kneusel RE, Matern U, Derewenda ZS.
    Journal: Acta Crystallogr D Biol Crystallogr; 1996 Nov 01; 52(Pt 6):1194-5. PubMed ID: 15299584.
    Abstract:
    A novel esterase obtained from Bacillus subtilis and capable of hydrolyzing the phytotoxin brefeldin A was crystallized using the hanging-drop technique. The crystals have two forms and both are monoclinic: form I, space group P2(1) with a = 101.7, b = 64.1, c = 55.4 A and beta = 102.5 degrees, and form II, space group C2 with a = 140.7, b = 82.6, c = 81.5 A and beta = 112.5 degrees. There are two molecules related by a pronounced non-crystallographic dyad per asymmetric unit in both crystal forms. The crystals diffract to 2.3 A using a rotating-anode X-ray source.
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