CRYSTALLIZATION AND PRELIMINARY STRUCTURAL STUDIES OF LACTOSE-SPECIFIC ENZYME IIA FROM LACTOCOCCUS-LACTIS

Citation
P. Sliz et al., CRYSTALLIZATION AND PRELIMINARY STRUCTURAL STUDIES OF LACTOSE-SPECIFIC ENZYME IIA FROM LACTOCOCCUS-LACTIS, Acta crystallographica. Section D, Biological crystallography, 52, 1996, pp. 1199-1201
Citations number
13
Language
INGLESE
art.tipo
Article
Categorie Soggetti
Crystallography,"Biochemical Research Methods",Biology
ISSN journal
0907-4449
Volume
52
Year of publication
1996
Part
6
Pages
1199 - 1201
Database
ISI
SICI code
0907-4449(1996)52:<1199:CAPSSO>2.0.ZU;2-M
Abstract
Lactose-specific enzyme IIA of the phosphoenol:pyruvate-dependent suga r phosphotransferase system from Lactococcus lactis has been crystalli zed in phosphate buffer. The crystals belong to space group P4(1)2(1)2 or its enantiomorph P4(3)2(1)2 with unit-cell axes a = b = 90.9 and c = 82.4 Angstrom. The packing parameter (Matthews parameter) V-m of 2. 48 Angstrom(3) Da(-1) is consistent with one trimer per asymmetric uni t and non-crystallographic threefold symmetry has been confirmed by ca lculating a self-rotation function. The crystals diffract X-rays to at least 2.3 Angstrom resolution, are stable in an X-ray beam and are th erefore appropriate for structure determination. Native data to 2.3 An gstrom resolution have been collected using a MAR image-plate system a t a synchrotron source. One isomorphous heavy-atom derivative has been identified and the presence of an isomorphous signal in the data has been confirmed by Patterson methods.