Crystallization and preliminary crystallographic data of SnoaL, a polyketide cyclase in nogalamycin biosynthesis




Sultana A, Kallio P, Jansson A, Niemi J, Mantsala P, Schneider G

PublisherBLACKWELL MUNKSGAARD

2004

 Acta Crystallographica Section D: Biological Crystallography

ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY

ACTA CRYSTALLOGR D

60

1118

1120

3

0907-4449

DOIhttps://doi.org/10.1107/S090744490400705X



Nogalonic acid methyl ester cyclase (SnoaL) catalyzes the last ring-closure step in the biosynthesis of the polyketide antibiotic nogalamycin. Crystals of a complex of SnoaL with the substrate nogalonic acid methyl ester have been obtained using PEG 4000 as precipitant. The crystals are orthorhombic, space group I222, with unit-cell parameters a = 69.1, b = 72.0, c = 65.4 Angstrom. They diffract to 1.35 Angstrom resolution using synchrotron radiation. A Matthews coefficient of 2.0 Angstrom(3) Da(-1) suggests one subunit in the asymmetric unit. Diffraction data for an isomorphous uranium derivative were collected and a difference Patterson map showed strong peaks which allowed determination of the position of the uranium ions.



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