4.1.1.11	-	
4.1.1.11	both apo form and in complex with isoasparagine	
4.1.1.11	co-crystallization of fully activated PanD and PanZ in complex, in a 10:11 PanD:PanZ ratio (protomer to monomer), hanging drop vapor diffusion method, mixing of 0.003 ml of 9 mg/ml protein in 50 mM Tris, 100 mM NaCl, and 0.1 mM DTT, pH 7.5, with 00.001 ml of reservoir solution containing 200 mM KSCN, 100 mM Bis-Tris propane, pH 6.5, and 20% w/v PEG 3350 at 18°C, X-ray diffraction structure determination and analysis at 1.16 A resolution. The same structure is observed using both room-temperature and cryo-cooled crystals, indicating that the hydrate is formed from the pyruvoyl cofactor and is not an intermediate in the activation reaction. This state is stabilized by a hydrogen bond to the amide of Gly24, which is held in place by interactions with PanZ	
4.1.1.11	crystal structure at 2.2. A resolution	
4.1.1.11	crystal structure of an unprocessed native proenzyme and of the mutants G24S, S25A, S25C, S25T, H11A, Ala-24 and Ala-26 insertion mutants, hanging-drop vapour-diffusion method	
4.1.1.11	purified recombinant His-tagged unprocessed, native precursor ADC, vapor diffusion hanging drop method, the precipitant solution contains 0.1 M sodium cacodylate, pH 6.5, 1.5 M magnesium sulfate, and 20% w/v PEG 2000, 15 days, cryoprotection by 20% v/v glycerol, X-ray diffraction structure determination and analysis at 2.99 A resolution	
4.1.1.11	purified recombinant mutant N72A, hanging drop vapour diffusion method, mixing of 0.001 ml of 19 mg /ml protein in 50 mM Tris-HCl, pH 8.0, with 0.001 ml of reservoir solution containing 1.6 M ammonium sulfate, pH 4.0, and equilibration against 0.5 ml of reservoir solution, 19°C, 3 days, cryoprotection by 1.8 M ammonium sulfate, 0.1 M citric acid, 30% glycerol pH 4.0 using 5% increments in glycerol concentration to prevent crystal dissolution, X-ray diffraction structure determination and analysis at 1.7 A resolution	
4.1.1.11	purified recombinant protein complex PanD-PanZ-AcCoA, protein complexes are prepared with a 10:11 ratio of PanD to PanZ at a total protein concentration of 9-11 mg/ml, and a 2fold molar excess (with respect to PanZ) of acetyl-CoA. Crystals are obtained in 20% w/v PEG 3350, 0.1 M Bis-Tris propane, pH 7.4, and 0.2 M potassium thiocyanate, X-ray diffraction structure determination and analysis at 1.6 A resolution	
4.1.1.11	purified recombinant T57V mutant enzyme, hanging drops by vapour diffusion with a 1:1 ratio of protein to precipitant, 7.5 mg/ml protein, 1.5-3.4 M sodium malonate, pH 4.0, method optimization, 17°C, X-ray diffraction structure determination and analysis at 1.62 A resolution, modeling	
4.1.1.11	recombinant enzyme in the presence of the substrate analogue isoasparagine, hanging-drop vapour-diffusion method, X-ray analysis