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- Publisher
- Wiley
- Copyright
- Copyright © 2006 Wiley Subscription Services, Inc., A Wiley Company
- ISSN
- 1744-3091
- eISSN
- 1744-3091
- DOI
- 10.1107/S1744309106017039
- pmid
- 16754986
- Publisher site
- See Article on Publisher Site
Abstract
The enoyl‐acyl carrier protein (ACP) reductase from Streptococcus pneumoniae (FabK; EC 1.3.1.9) is responsible for catalyzing the final step in each elongation cycle of fatty‐acid biosynthesis. Selenomethionine‐substituted FabK was purified and crystallized by the hanging‐drop vapour‐diffusion method at 277 K. The crystal belongs to space group P21, with unit‐cell parameters a = 50.26, b = 126.70, c = 53.63 Å, β = 112.46°. Diffraction data were collected to 2.00 Å resolution using synchrotron beamline BL32B2 at SPring‐8. Two molecules were estimated to be present in the asymmetric unit, with a solvent content of 45.1%.
Journal
Acta Crystallographica Section F – Wiley
Published: Jun 1, 2006