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Title
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The purification, crystallization and preliminary diffraction of a glycerophosphodiesterase from Enterobacter aerogenes.
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Authors
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C.J.Jackson,
P.D.Carr,
H.K.Kim,
J.W.Liu,
D.L.Ollis.
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Ref.
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Acta Crystallogr Sect F Struct Biol Cryst Commun, 2006,
62,
659-661.
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PubMed id
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Abstract
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The metallo-glycerophosphodiesterase from Enterobacter aerogenes (GpdQ) has been
cloned, expressed in Escherichia coli and purified. Initial screening of
crystallization conditions for this enzyme resulted in the identification of
needles from one condition in a sodium malonate grid screen. Removal of the
metals from the enzyme and subsequent optimization of these conditions led to
crystals that diffracted to 2.9 angstroms and belonged to space group P2(1)3,
with unit-cell parameter a = 164.1 angstroms. Self-rotation function analysis
and V(M) calculations indicated that the asymmetric unit contains two copies of
the monomeric enzyme, corresponding to a solvent content of 79%. It is intended
to determine the structure of this protein utilizing SAD phasing from transition
metals or molecular replacement.
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