3.7.1.8	at 2.4 A resolution, active-site residues are Ser110, Asp235 and His263, situated inside the cavity between the core and the lid domains, this substrate binding pocket has a hydrophobic and hydrophilic region	
3.7.1.8	BphD H265Q and S112A/H265Q mutants in complex with substrate 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid, sitting drop vapour diffusion method, 0.001 ml of protein solution containing 4 mg/ml protein in 20 mM HEPES, pH 7.5, 20°C, 9 days, is mixed with 0.001 ml of reservoir solution containing 2.4 M malonate at pH 6.0-7.0, X-ray diffraction structure determination and analysis at 1.3 A and 1.9 A resolutions, respectively	
3.7.1.8	enzyme structure determination and analysis, PDB ID 1C4X	
3.7.1.8	enzyme structure determination and analysis, PDB IDs 2OG1, 2PU5, 2RI6, 2PU7, 2PUH and 2PUJ	
3.7.1.8	H263 mutant by hanging drop vapor diffusion, to 2 A resolution	
3.7.1.8	mutant S114A in complex with 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid, 8-(2-chlorophenyl)-2-hydroxy-5-methyl-6-oxoocta-2,4-dienoic acid, or 4,5-9,10-diseco-3-hydroxy-5,9,17-trioxoandrosta-1(10),2-diene-4-oic acid, sitting drop vapor diffusion, 0.001 ml of 8 mg/ml protein solution is mixed with 0.001 ml of precipitant solution containing 200 mM KSCN, 24% PEG 3350, and 100 mM bis-tris propane, pH 7.0, soaking of S114A crystals in 0.01 ml of precipitant solution supplemented with 15 mM of each ligand for 30-60 min, X-ray diffractin structure determination and analysis at 1.8-2.1 A resolution, molecular replacement	
3.7.1.8	S112A and H265Q mutants crystal structure analysis, PDB IDs 2PUH and 3V1N, modeling	
3.7.1.8	wild-type, the S112C variant and S112C incubated with 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid by hanging drop vapor diffusion method at 20°C, to 1.6 A resolution, interaction between conserved active side residues and dienoate moiety of the substrate, the residue His265 is hydrogen-bonded to the 2-hydroxy/oxo substituent of the substrate, consistent with a role in catalyzing ketonization