Crystallization and preliminary X-ray analysis of the inducible lysine decarboxylase from Escherichia coli.
The decameric inducible lysine decarboxylase (LdcI) from Escherichia coli has been crystallized in space groups C2 and C222(1); the Ta6Br12(2+) cluster was used to derivatize the C2 crystals. The method of single isomorphous replacement with anomalous scattering (SIRAS) as implemented in SHELXD was used to solve the Ta6Br12(2+)-derivatized structure to 5 A resolution. Many of the Ta6Br12(2+)-binding sites had twofold and fivefold noncrystallographic symmetry. Taking advantage of this feature, phase modification was performed in DM. The electron-density map of LdcI displays many features in agreement with the low-resolution negative-stain electron-density map [Snider et al. (2006), J. Biol. Chem. 281, 1532-1546].
Alexopoulos
Eftichia
E
Department of Biochemistry, University of Toronto, 1 King's College Circle, Medical Sciences Building, Toronto, Ontario M5S1A8, Canada.
Kanjee
Usheer
U
Snider
Jamie
J
Houry
Walid A
WA
Pai
Emil F
EF
D002262:Carboxy-Lyases / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D002850:Chromatography, Gel; D003460:Crystallization; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000201:enzymology*; D011487:Protein Conformation
D002262:Carboxy-Lyases; C021520:lysine decarboxylase