CRYSTALLIZATION AND PRELIMINARY DIFFRACTION STUDIES OF FIREFLY LUCIFERASE FROM PHOTINUS-PYRALIS

Authors
CONTI E LLOYD LF AKINS J FRANKS NP BRICK P
Citation
E. Conti et al., CRYSTALLIZATION AND PRELIMINARY DIFFRACTION STUDIES OF FIREFLY LUCIFERASE FROM PHOTINUS-PYRALIS, Acta crystallographica. Section D, Biological crystallography, 52, 1996, pp. 876-878
Citations number
18
Categorie Soggetti
Crystallography,"Biochemical Research Methods",Biology
Journal title
Acta crystallographica. Section D, Biological crystallography → ACNP
ISSN journal
09074449
Volume
52
Year of publication
1996
Part
4
Pages
876 - 878
Database
ISI
SICI code
0907-4449(1996)52:<876:CAPDSO>2.0.ZU;2-1
Abstract
Firefly luciferase is a 62 kDa molecular weight enzyme which catalyzes a light-emitting reaction. Crystals of Photinus pyralis luciferase ha ve been obtained by the microbatch technique, using polyethylene glyco l as a precipitating agent. Firefly luciferase crystallizes as long ne edles which belong to the tetragonal space group P4(1)2(1)2, with cell dimensions a = 119.5, b = 119.5, c = 95.4 Angstrom. One molecule is p resent in the asymmetric unit. Diffracted intensities beyond 2.0 Angst rom resolution have been measured from frozen crystals using synchrotr on radiation.