Some forms of this enzyme will also use geranyl diphosphate and dimethylallyl diphosphate as donors; it will not use larger prenyl diphosphates as efficient donors.
Some forms of this enzyme will also use geranyl diphosphate and dimethylallyl diphosphate as donors; it will not use larger prenyl diphosphates as efficient donors.
the enzyme structure harbors eleven alpha-helices typical for the FPP synthase family enzymes, the enzyme structure contains two DDxxD motifs and three Mg2+ ions
the enzyme structure harbors eleven alpha-helices typical for the FPP synthase family enzymes, the enzyme structure contains two DDxxD motifs and three Mg2+ ions
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant wild-type of selenomethionine-labeled enzyme, 20 mg/mL protein in 10 mM Tris-HCl, pH 7.9, 10 mM MgCl2, 100 mM NaCl, and 0.5 mM tris(2-carboxyethyl)phosphine, crystals of SeMet-labeled enzyme are obtained by vapor diffusion with hanging drops that contain a 1:1 mixture of protein solution and reservoir buffer D, the latter containing 100 mM sodium acetate, pH 4.4, 40% v/v propanediol, 10 mM MgCl2, and 0.5 mM TCEP, liquid nitrogen freezing without the addition of a cryo protectant, a second crystal form is obtained with native enzyme using the same procedure but with reservoir buffer E containing 100 mM N-cyclohexyl-3-aminopropane sulfonic acid, pH 10.0, 200 mM NaCl, 9-11% PEG 8000, 10 mM MgCl2, and 0.5 mM TCEP, mixing with reservoir buffer E containing 30% v/v glycerol and flash-freezing in liquid nitrogen, X-ray diffraction structure determination and analysis at 1.8-2.0 A resolution, multiwavelength anomalous diffraction, soaking of native enzyme with FPP and Mg2+ fails, overview