Crystallization of a novel esterase which inactivates the macrolide toxin brefeldin A.
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.
Department of Molecular Physiology and Biological Physics, University of Virginia, Charlottesville 22908, USA.
Y
Y
Wei
L
L
Swenson
R E
RE
Kneusel
U
U
Matern
Z S
ZS
Derewenda