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 - 10 of 17 > >>
EC Number Crystallization (Commentary) Reference
Show all pathways known for 3.6.1.13Display the word mapDisplay the reaction diagram Show all sequences 3.6.1.13- 667690
Show all pathways known for 3.6.1.13Display the word mapDisplay the reaction diagram Show all sequences 3.6.1.13complexed with 8-oxo-dGMP, 8-oxo-dGDP and 8-oxo-dADP, hanging drop vapor diffusion method, using 0.8 M NaH2PO4/1.2M K2HPO4 and 0.1 M acetate (pH 4.5), and 0.2M ammonium acetate, 35-40% (w/v) polyethylene glycol 3350 and 0.1 M sodium citrate (pH 6.2) 741073
Show all pathways known for 3.6.1.13Display the word mapDisplay the reaction diagram Show all sequences 3.6.1.13crystal structures analysis of Ndx4 in the E-state obtained at 0.91 A resolution, PDB IDs are 2YVM, 1MP2, 1G0S, and 2DSB 756035
Show all pathways known for 3.6.1.13Display the word mapDisplay the reaction diagram Show all sequences 3.6.1.13crystallized in absence or presence of ADP-ribose by hanging-drop vapour-diffusion method. 1.5 A resolution from the apo form using synchrotron radiation and 2.0 A resolution from the complexed form. Both crystals belong to space group P3(1)21 or P3(2)21 and contain one molecule in the asymmetric unit 654079
Show all pathways known for 3.6.1.13Display the word mapDisplay the reaction diagram Show all sequences 3.6.1.13gadolinium derivative, to 2.0 A resolution. The crystal structure of DR2204 consists of the conserved alpha/beta/alpha sandwich fold typical of Nudix hydrolases, the Nudix box, residues 94-115, holding the alpha1 helix sits between two loops accessible to the solvent, while the other two helices, alpha2 and alpha3, lie on the other side of the central beta-sheet and participate in dimer-interface formation 710725
Show all pathways known for 3.6.1.13Display the word mapDisplay the reaction diagram Show all sequences 3.6.1.13hanging-drop vapor diffusion at 18°C. The structure of the apo enzyme, the active enzyme and the complex with ADP-ribose are determined to 1.9 A, 2.7 A and 2.3 A, respectively. The Nudix motif residues, folded as a loop-helix-loop tailored for diphosphate hydrolysis, compose the catalytic center 656856
Show all pathways known for 3.6.1.13Display the word mapDisplay the reaction diagram Show all sequences 3.6.1.13in apo form, in complex with ADP-D-ribose, and in complex with AMP with bound Mg2+, hanging drop vapor diffusion method, using 160 mM sodium acetate (pH 5.5), and 25% (w/v) 2-methyl-2,4-pentanediol, or 300 mM di-ammonium hydrogen citrate, 6% (w/v) n-propanol and 15% (w/v) polyethylene glycol 3350, or 200 mM sodium acetate, 100 mM Tris-HCl (pH 8.0) and 30% (w/v) polyethylene glycol 4000 715902
Show all pathways known for 3.6.1.13Display the word mapDisplay the reaction diagram Show all sequences 3.6.1.13in complex with alpha,beta-methyleneadenosine diphosphoribose and 3 Mg2+ ions, hanging drop vapor diffusion method, using 250 mM sodium acetate, 100 mM Tris-HCl, pH 8.0, and 29% (w/v) polyethylene glycol 4000 688413
Show all pathways known for 3.6.1.13Display the word mapDisplay the reaction diagram Show all sequences 3.6.1.13in complex with alpha,beta-methyleneadenosine diphosphoribose, sitting drop vapor diffusion method, using 18% (w/v) PEG 4000, 0.1 M sodium acetate buffer pH 5.3, 20% (w/v) glycerol, 0.2 M ammonium sulfate, at 20°C 718517
Show all pathways known for 3.6.1.13Display the word mapDisplay the reaction diagram Show all sequences 3.6.1.13Ndx2 alone and in complex with Mg2+, with Mg2+ and AMP, and with Mg2+ and a nonhydrolyzable ADPR analogue, hanging-drop vapor diffusion method, 20 mg/ml protein in 20 mM Tris-HCl, pH 8.0, and 100 mM KCl, 0.001 ml of protein solution is mixed with the equal volume of reservoir solution and equilibrated against the reservoir, containing 0.1 M MES, pH 6.5, 0.16 M sodium acetate or magnesium acetate for the complexed enzyme, 14% PEG 8000, and 20% glycerol, at 20°C, soaking of crystals in 50 mM KAu(CN)2, X-ray diffraction structure determination and anaylsis at 2.0 A resolution, MAD phasing, model building, and refinement 687404
Results 1 - 10 of 17 > >>