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

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].

SUBMITTER: Alexopoulos E

PROVIDER: S-EPMC2494963 | biostudies-literature | 2008 Aug

REPOSITORIES: biostudies-literature

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

Alexopoulos Eftichia E Kanjee Usheer U Snider Jamie J Houry Walid A WA Pai Emil F EF

Acta crystallographica. Section F, Structural biology and crystallization communications 20080705 Pt 8

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, ph ...[more]

PMID: 18678936

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