Inititiating a structural study of 2-keto-3-deoxy-6-phosphogluconate aldolase from Escherichia coli

LV Buchanan, N Mehta, S Pocivavsek, S Niranjanakumari, EJ Toone, James Henderson Naismith

Research output: Contribution to journalArticlepeer-review

4 Citations (Scopus)


2-Keto-3-deoxy-6-phosphogluconate aldolase (KDPG aldolase, E.C. 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 Angstrom 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 Angstrom.

Original languageEnglish
Pages (from-to)1946-1948
Number of pages3
JournalActa Crystallographica. Section D, Biological crystallography
Publication statusPublished - Nov 1999




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