Initiating a structural study of 2-keto-3-deoxy-6-phosphogluconate aldolase from Escherichia coli.
Journal Article
2-Keto-3-deoxy-6-phosphogluconate aldolase (KDPG aldolase, E.C. 4.1. 2.14) is a member of the pyruvate/phosphoenolpyruvate aldolase family. It is also a synthetically useful enzyme, capable of catalyzing the stereoselective aldol addition of pyruvate to a range of unnatural electrophilic substrates. The recombinant protein was purified by a two-step HPLC protocol involving anion-exchange and hydrophobic chromatography. Dynamic light-scattering experiments indicated the protein to be monodisperse. Crystals were obtained using the sitting-drop vapour-diffusion method, with PEG 6K as precipitant. Diffraction data were collected on a frozen crystal to a resolution of 2.26 A on station PX9.6 at the Daresbury synchrotron. The crystal belongs to space group P2(1)2(1)2(1), with unit-cell parameters a = 53.2, b = 77.9, c = 146.8 A.
Full Text
Duke Authors
Cited Authors
- Buchanan, LV; Mehta, N; Pocivavsek, L; Niranjanakumari, S; Toone, EJ; Naismith, JH
Published Date
- November 1999
Published In
Volume / Issue
- 55 / Pt 11
Start / End Page
- 1946 - 1948
PubMed ID
- 10531504
Pubmed Central ID
- 10531504
Electronic International Standard Serial Number (EISSN)
- 1399-0047
International Standard Serial Number (ISSN)
- 0907-4449
Digital Object Identifier (DOI)
- 10.1107/s0907444999011166
Language
- eng