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 5–12% poly(ethylene glycol) 900 and 100 mM sodium phosphate/citrate buffer, pH 3.6–4.1. Crystallization of the enzyme after incubation with ATP or ADP and Mn2+. Co-crystal structures of Rio2–ATP–Mn and Rio2–ADP–Mn 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	
2.7.11.1	purified recombinant wild-type and selenomethionine-labeled Rio2, hanging drop vapour diffusion method, equal volumes of protein solution, containing 5-12% PEG 900, and 0.1 M phosphate citrate buffer, pH 3.6-4.1, and reservoir solution, versus 1 ml reservoir solution, purified recombinant Rio2 complexed with ATP using 0.1 M Tris, pH 7.5, 20 mM ATP, 20 mM MgCl2, 20 mM adenosine 5'-(beta,gamma-imino)triphosphate, and 20% ethylene glycol, 20°C, 2-4 days, X-ray diffraction structure determination and analysis at 2.0 A resolution	663404	
2.7.11.1	sitting-drop vapour-diffusion method at 16°C. The structure of PpkA-294 is determined in its apo form to a 1.6 A resolution as well as in complex with ATP to a 1.41 A resolution and with an ATP analogue AMP-PCP to a 1.45 A resolution. The residues in the activation loop of PpkA-294 are fully determined, and the N-terminus of the loop is folded into an unprecedented inhibitory helix, revealing that the PpkA kinase domain is in an autoinhibitory state	760526	
2.7.11.1	sitting-drop variant of the vapour-diffusion method	726563	
2.7.11.1	the structures of the catalytic subunit of protein kinase CK2 from Zea mays complexed with Mg2+ and with analogs of ATP or GTP are determined to 2.2 A resolution	728361	
2.7.11.1	truncation mutant of CKI delta lacking the C-terminal autoinhibitory region	491629	
2.7.11.1	vapor diffusion method, crystal structures of PknI sensor domain (PknI_SD) monomer and dimer, as well as PknI kinase domain (PknI_KD)	762484	
2.7.11.1	X-ray crystal structure of toyocamycin bound to Rio1 at 2.0 A, toyocamycin binds in the ATP binding pocket of the protein	723566