4.1.1.98	hanging drop vapor diffusion method, using 15% (w/v) PEG 4000, 0.2 M LiSO4, and 0.1 M Hepes buffer (pH 7.0)	730891	
4.1.1.98	purified recombinant His6-tagged wild-type (FMN-bound) and V47S mutant (FMN-free) enzymes, hanging drop vapour diffusion method, mixing of 800 nl of 21 mg/ml protein solution with 800 nl of reservoir solution containing 200 mM sodium chloride, 100 mM potassium phosphate monobasic/sodium phosphate dibasic, pH 5.8, and 11% w/v PEG 8000, for the wild-type enzyme and 0.1 M trisodium citrate, pH 5.4, 0.5 M ammonium sulfate, and 1.2 M lithium sulfate for the mutant enzyme, 20°C, 3 days, method optimization, X-ray diffraction structrue determination and analysis at 2.0 A and 1.76 A resolution, respectively	746643	
4.1.1.98	sitting drop vapor diffusion method, using 0.1 M trisodium citrate pH 5.4, 0.5 M ammonium sulfate, 1.2 M lithium sulfate	728916	
4.1.1.98	sitting drop vapor diffusion method, using 1 M (NH4)2SO4, 0.1 M Bis-Tris, pH 5.5, 1% (w/v) PEG 3350 or 0.1 M HEPES, pH 7.5, 0.2 M MgCl2, 10% (w/v) PEG 400	730732	
4.1.1.98	structures of an FMN-bound wild type form and an FMN-unbound V47S mutant form. UbiX is a dodecameric enzyme, and each monomer possesses a typical Rossmann-fold structure. The FMN-binding domain of UbiX is composed of three neighboring subunits. The highly conserved Gly15, Ser41, Val47, and Tyr171 residues play important roles in FMN binding. The FMN-bound wild type form and the FMN-free form show a significant conformational difference in the C-terminal loop region (comprising residues 170-176 and 195-206)	749310	
4.1.1.98	structures of holoUbiD reveal a relatively open active site potentially occluded from solvent through domain motion	748226