Crystallization and preliminary X-ray analysis of the inducible lysine decarboxylase from Escherichia coli
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The decameric inducible lysine decarboxylase (LdcI) from Escherichia coli has been crystallized in space groups C2 and C222{sub 1}; the Ta{sub 6}Br{sub 12}{sup 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 Ta{sub 6}Br{sub 12}{sup 2+}-derivatized structure to 5 {angstrom} resolution. Many of the Ta{sub 6}Br{sub 12}{sup 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].
- Research Organization:
- Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
- Sponsoring Organization:
- USDOE
- OSTI ID:
- 1006713
- Journal Information:
- Acta Crystallogr. F, Vol. 64, Issue (8) ; 08, 2008; ISSN 1744-3091
- Country of Publication:
- United States
- Language:
- ENGLISH
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