Any feedback?
Please rate this page
(search_result.php)
(0/150)

BRENDA support

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 - 7 of 7
EC Number Crystallization (Commentary)
Show all pathways known for 4.1.1.9Display the word mapDisplay the reaction diagram Show all sequences 4.1.1.9-
Show all pathways known for 4.1.1.9Display the word mapDisplay the reaction diagram Show all sequences 4.1.1.9hanging drop vapour-diffusion method, X-ray analysis
Show all pathways known for 4.1.1.9Display the word mapDisplay the reaction diagram Show all sequences 4.1.1.9purified recombinant detagged enzyme, from 15% PEG 2000 monomethyl ether and 0.1 M sodium acetate, pH 4.5, and 10 mM sodium citrate, sitting drop vapor diffusion method, X-ray diffraction structure determination and analysis at 3.3-4.3 A resolution, molecular replacement
Show all pathways known for 4.1.1.9Display the word mapDisplay the reaction diagram Show all sequences 4.1.1.9purified recombinant enzyme, microbatch method, 0.002 ml of the protein solution containing 10 mM Tris, pH 7.5, 100 mM NaCl, 5 mM DTT, and 0.02% NaN3 are mixed with 0.002 ml of the precipitant solution consisting of 0.1 M magnesium nitrate, 100 mM Tris, pH 8.5, and 33% v/v PEG 400, 18°C, X-ray diffraction structure determination and analysis at 2.3-3.1 A, selenomethionyl single-wavelength anomalous diffraction method, molecular replacement
Show all pathways known for 4.1.1.9Display the word mapDisplay the reaction diagram Show all sequences 4.1.1.9purified recombinant enzyme, microbatch method, 0.002 ml of the protein solution containing 10 mM Tris, pH 7.5, 100 mM NaCl, 5 mM DTT, and 0.02% NaN3 are mixed with 0.002 ml of the precipitant solution consisting of 200 mM ammonium sulfate, and 20% w/v PEG3350, 18°C, X-ray diffraction structure determination and analysis at 2.3-3.1 A, selenomethionyl single-wavelength anomalous diffraction method, molecular replacement
Show all pathways known for 4.1.1.9Display the word mapDisplay the reaction diagram Show all sequences 4.1.1.9purified recombinant enzyme, microbatch method, mixingof 0.002 ml of protein in 20 mM Tris, pH 7.0, 250 mM NaCl, 5% v/v glycerol, and 3 mM malonyl-CoA with crystallization solution containing 160 mM magnesium chloride, 80 mM Tris, pH 8.5, 24% w/v PEG 4000, 20% v/v glycerol, and 3% v/v ethanol, 18°C, X-ray diffraction structure determination and analysis at 2.3-3.1 A, selenomethionyl single-wavelength anomalous diffraction method, molecular replacement
Show all pathways known for 4.1.1.9Display the word mapDisplay the reaction diagram Show all sequences 4.1.1.9recombinant mutant E58A/K59A/E278A/E279A/K280A, sitting-drop vapor diffusion method, mixing of 10 mg/ml protein in HEPES, pH 7.5, 100 mM NaCl, 1% v/v glycerol, and 5 mM decanoyl-CoA. in a 2:1 ratio with a precipitant solution containing 10% w/v PEG 20000 and 0.1 M 2-(N-morpholino)ethanesulfonic acid, pH 6.0, at room temperature, X-ray diffraction structure determination and analysis at 2.8 A, by single isomorphous replacement with anomalous scattering
Results 1 - 7 of 7