Refine search

Search Crystallization (Commentary)

show results
Don't show organism specific information (fast!)
Search organism in taxonomic tree (slow, choose "exact" as search mode, e.g. "mammalia" for rat,human,monkey,...)
(Not possible to combine with the first option)
Refine your search

Search term:

Results 1 - 10 of 10
EC Number
Crystallization
Reference
co-crystallization of L-cysteine and purified wild-type cysteine dioxygenase by the hanging drop, vapor-diffusion method at 16°C, the crystals grow as rods up to 0.2 x 0.2 x 0.8 mm in 1 week. Refinement of the crystal stucture leads to a final model with a crystallographic R-factor of 18.1% and a free R-factor of 21.5% at 2.7 A resolution.
crystallization in sitting drops at 25°C using a reservoir of 0.1-0.25 M ammonium acetate, 0.1 M tri-sodium citrate, pH 5.6, with 22-26% (w/v) polyethylene glycol 4000. The co-crystals with 5 mM are grown using a reservoir of 0.15 M ammonium sulfate, 0.2 M sodium cacodylate, pH 6.5, with 26% (w/v) polyethylene glycol 8000. The crystal sturcture, solved by SAD phasing using selenomethionine-substituted protein, yields a final refined model with r = 18.0 and Rfree = 20.8 at 1.5-A resolution. Data from a co-crystallization experiment with 5 mM cysteine shows structural changes in the binding pocket, they are determined to 1.5 A resolution (final r = 19.8 and Rfree = 22.4).
crystals are grown at 25°C by hanging-drop vapor-diffusion. The reservoir contains 20% methosylpolyethylene glycol 5000, 160 mM CaCl2, and 100 mM 2-morpholinjoethane-sulfonic acid (pH 6.5). Hanging drops consist of 2 microl of protein solution mixed with 2 microl of reservoir solution. Structure is solved to a nominal 1.75 A resolution.
electron paramagnetic study of substrate-O2 binding. Ordered binding of L-cysteine prior to NO and presumably O2. Upon addition of NO to cysteine dioxygenase in the presence of substrate L-cysteine, a low-spin(FeNO)7 signal with spin S of 1/2that accounts for 85% of the iron within the enzyme develops. Substitution of L-cysteine with isosteric substrate analogues cysteamine, 3-mercaptopropionic acid, and propane thiol does not produce any analogous signals.The unusual (FeNO)7, spin 1/2 electronic configuration adopted by the substrate-bound iron-nitrosyl cysteine dioxygenase is a result of the bidentate thiol/amine coordination of L-cysteine in the NO-bound active site
enzyme with or without bound cysteine and formation of persulfenate, usage of crushed CDO crystals at 8 mg/mL in 10 mM Tris, pH 7.4, recrystallized by hanging drop vapour diffusion method, mixing of 0.0005 ml of crystal seed stock solution with 0.001 ml protein solution and 0.001 ml of reservoir solution containing 0.1 M trisodium citrate, pH 5.6, 24% PEG 4000, and 0.15 M ammonium acetate, final pH of 6.2, at room temperature, X-ray diffraction structure determination and analysis at pH 4.0-9.0 and 1.25-1.60 A resolution, overview
generation of 21 CDO crystal structures at resolutions between 1.25 and 1.65 A. Of these, 16 are of C93A or Y157F CDO mutants either alone or bound to L-Cys, D-Cys, or the inhibitor homocysteine, the other five are of wild-type CDO bound to homocysteine, azide, or thiosulfate. Cys-soaked wild-type CDO crystals are analysed at pH 6.2 and pH 8.0, detailed overview
purified enzyme, hanging drop vapour diffusion method, mixing of 0.0015 ml of 7 mg/mL CDO mutant C93G in 10 mM sodium phosphate and 20 mM NaCl, pH 7.5, and 0.0006 ml of crushed wild-type CDO crystal seeds in their own growth solution consisting of 25% w/v PEG 1500, 13 mM succinate, 44 mM sodium phosphate, and 44 mM glycine, pH 5.2, with 0.0015 ml of reservoir buffer containing 26% w/v PEG 4000, 200 mM ammonium acetate, and 100 mM sodium citrate, pH 6.3, equilibration against reservoir solution, X-ray diffraction structure determination and analysis at 1.82 A resolution
purified recombinant enzyme complexed with cysteine persulfide or 3-mercaptopropionic acid persulfide, hanging drop vapor diffusion method, mixing of 0.0015 ml of 8 mg/ml protein with 0.0015 ml of reservoir solution containing 24-34% w/v PEG 4000, 100-250 mM ammonium acetate, 100 mM sodium citrate, pH 5.6, 0-4 mM dithionite, and 40 mM ligand, final pH is 6.1-6.2, 24°C, one week, X-ray diffraction structure determination and analysis at 1.63-2.05 A resolution
purified recombinant enzyme free or with bound substrate L-Cys, hanging drop vapour diffusion method, mixing of 0.004 ml of 10 mg/ml protein solution with 0.004 ml of reservoir solution containing 18% w/v PEG 4000, 0.1 M potassium acetate, 0.05 M 2-(N-morpholino)ethanesulfonic acid, pH 6.0, 25°C, 2-7 days, X-ray diffraction structure determination and analysis at 2.38-2.82 A resolution
X-ray crystal structure
Results 1 - 10 of 10