PMID:10531504
| Citation |
Buchanan, LV, Mehta, N, Pocivavsek, L, Niranjanakumari, S, Toone, EJ and Naismith, JH (1999) Initiating a structural study of 2-keto-3-deoxy-6-phosphogluconate aldolase from Escherichia coli. Acta Crystallogr. D Biol. Crystallogr. 55:1946-8 |
|---|---|
| Abstract |
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. |
| Links | |
| Keywords |
Aldehyde-Lyases/chemistry; Amino Acid Sequence; Crystallization; Escherichia coli; Molecular Sequence Data; Polyethylene Glycols/pharmacology; Protein Conformation; Pseudomonas putida; Recombinant Proteins/chemistry; Scattering, Radiation; Selenomethionine/chemistry; Sequence Homology, Amino Acid; X-Ray Diffraction |
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