EC Number |
Reference |
---|
2.7.11.1 | - |
491320, 491614, 762489 |
2.7.11.1 | autoinhibitory junction region bound to the calmodulin-like domain and Ca2+, 20 mg/ml protein in 20 mM Tris buffer, pH 7.0, 10 mM CaCl2, 10 mM DTT, mixed with an equal volume of precipitating agent composed of 15% w/v PEG 400, 0.1 M calcium chloride, and 0.1 M sodium acetate at pH 7.6, equilibration against a reservoir of precipitating agent by vapour diffusion at 20°C, X-ray diffraction structure determination and anaylsis at 2.0 A resolution, multiple-wavelength anomalous dispersion |
675373 |
2.7.11.1 | crystallized by vapour diffusion method. Crystal structure, at 2.1 A resolution, of recombinant alpha subunit of protein kinase CK2a in the presence of ATP and Mg2+, shows the enzyme in an active conformation stabilized by interactions of the N-terminal region with the activation segment and with a cluster of basic residues known as the substrate recognition site. The active centre is occupied by a partially disordered ATP molecule with the adenine base attached to a novel binding site of low specificity. This finding explains the observation that CK2, unlike other protein kinases, can use both ATP and GTP as phosphorylating agents |
727360 |
2.7.11.1 | hanging drop vapor diffusion in 1 ml wells containing 512% poly(ethylene glycol) 900 and 100 mM sodium phosphate/citrate buffer, pH 3.64.1. Crystallization of the enzyme after incubation with ATP or ADP and Mn2+. Co-crystal structures of Rio2ATPMn and Rio2ADPMn are solved at 1.84 and 1.75 A resolution, respectively |
722223 |
2.7.11.1 | hanging drop vapor diffusion method, high resolution crystal structures of Archaeoglobus fulgidus Rio1 in the presence and absence of bound nucleotides |
722224 |
2.7.11.1 | microbatch-under-oil method, using 100 mM Bis-Tris (pH 6.5), 28% (w/v) PEG 2000 |
739722 |
2.7.11.1 | purified enzyme mutant, mixing of 25 nl 11 mg/ml protein with 0.9 mM inhibitor delalisib in 20 mM Tris, pH 7.2, 50 mM (NH4)2SO4, 1% v/v ethylene glycol, 1% w/v betaine, 300 mM CHAPS, and 5 mM TCEP, with 25 nl of reservoir solution containing 25% w/v PEG 3350, 0.1 M Bis-Tris, pH 6.5, microseeding in 480 nl of 2.5% w/v n-dodecyl-beta-D-maltoside, 300 nl of 20 mM ligand, and 0.12 ml of 12 mg/ml DELTAABD-p110delta in storage buffer 20 mM Tris, pH 7.2, 50 mM (NH4)2SO4, 1% v/v ethylene glycol, 1% w/v betaine, 300 nM CHAPS, and 5mM TCEP, X-ray diffraction structure determination and analysis at 2.4-2.5 A resolution |
738673 |
2.7.11.1 | purified recombinant His-tagged N-terminal catalytic domain of PknB, residues 1-331, hanging drop vapour diffusion method, 0.001 ml protein solution containing 5 mg/ml protein mixed with equal volume of 0.1 M HEPES, pH 7.5, 30 mM MgCl2, 0.15 mM inhibitor AMP-PNP, 27% PEG 400, and 4% 1,3-butanediol, 19°C, versus 1 ml of a solution containing 0.1 M HEPES, pH 7.5, 30 mM MgCl2, and 27% PEG 400, 2-3 weeks, X-ray diffraction structure determination and analysis at 2.2 A resolution |
662128 |
2.7.11.1 | purified recombinant Leu-Glu-His6-tagged GSK3beta in complex with ATP or ATP analogue AMP-PNP, 10 mg/ml protein, 2 mM ATP or AMP-PNP, 12-14% w/v PEG 6000, 100 mM NaCl, 5 mM MgCl2, 10% v/v glycerol, in 100 mM HEPES-NaOH, pH 7.5, hanging drop vapor diffusion method, 4°C, several days, soaking in 0.1 mM ethylmercuric thiosalyclate at pH 7.5 for 1 h, cryoprotection by 30% w/v D-sorbitol, X-ray diffraction structure determination and analysis at 1.7-2.6 A resolution |
660602 |
2.7.11.1 | purified recombinant low activity WNK1 mutant S382A, wild-type and selenomethionine-labeled, hanging drop vapour diffusion method, 16°C, mixing of 0.002 ml of protein solution and of well solution, the latter containing 24% PEG monomethyl ester 2000, 0.3 M NaCl, 0.1 M HEPES, pH 7.0-8.0, 3 days, stabilization with 15% glycerol, X-ray diffraction structure determination and analysis at 1.8 A resolution |
663401 |