NDLI: Crystallization and preliminary X-ray analysis of the inducible lysine decarboxylase from Escherichia coli.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Alexopoulos, Eftichia Kanjee, Usheer Snider, Jamie Houry, Walid A. Pai, Emil F.
Description	Country affiliation: Canada Author Affiliation: Alexopoulos E ( Department of Biochemistry, University of Toronto, 1 King's College Circle, Medical Sciences Building, Toronto, Ontario M5S1A8, Canada.)
Abstract	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].
File Format	HTM / HTML
ISSN	2053230X
e-ISSN	17443091
DOI	10.1107/S1744309108018757
Journal	Acta Crystallographica Section F Structural Biology and Crystallization Communications
Issue Number	Pt 8
Volume Number	64
Language	English
Publisher	Wiley
Publisher Date	2008-08-01
Publisher Place	Great Britain (UK)
Access Restriction	Open
Subject Keyword	Discipline Crystallography Discipline Biophysics Discipline Molecular Biology Discipline Biochemistry Carboxy-lyases Chemistry Escherichia Coli Enzymology Genetics Isolation & Purification Chromatography, Gel Crystallization Crystallography, X-ray Protein Conformation
Content Type	Text
Resource Type	Article
Subject	Genetics Structural Biology Medicine Biochemistry Biophysics Condensed Matter Physics

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