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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified enzyme IMP-2 MBL, hanging drop vapour diffusion metod, mixxing of 0.003 ml of 5 mg/ml protein in 20 mM HEPES-NaOH, pH 7.5, with 0.003 ml of reservoir solution containing 30% w/v PEG 4000, 0.1 M citric acid/sodium citrate, and 0.2 M sodium acetate, pH 6.0, equilibration against 0.35 ml reservori solution, 20°C, X-ray diffraction structure determination and analysis at 2.3 A resolution, modeling and structure comparisons
purified recombinant enzyme, hanging drop vapor diffusion method, mixing of 6 mg/ml protein in 10 mM HEPES, pH 7.5, with crystallization solution containing 0.1 M HEPES, pH 7.5, 0.1 M sodium acetate, and 28% PEG 2000, X-ray diffraction structure determination and analysis
hanging-drop vapor-diffusion method, crystals exhibit orthorhombic symmetry P2(1)2(1)2(1), with unit-cell parameters a = 40.75, b = 42.05, c = 128.88 A. There is one monomer in the asymmetric unit
purified recombinant enzyme, complexed with cefoxitin in an acyl-enzyme-adduct, for monoclinic crystals: 0.005 ml protein solution, 10 mg/ml, + equal volume of reservoir solution containing 25% PEG 6000, 0.1 M sodium acetate, pH 5.0, against 1 ml of reservoir solution at 20°C, for very big prismatic crystals: 40 mg/ml protein with lowered PEG 6000 concentration, pH 3.4, complexing by diffusion of cefoxitin for 24 h, X-ray diffraction structure determination and analysis at 1.7 A resolution
enzyme BlaB in complex with the inhibitor D-captopril, hanging drop method, 0.002 ml of 5 mg/ml protein in 10 mM sodium cacodylate, 0.1 mM zinc acetate, 0.1 mM DTT, pH 6.5, is mixed with 0.001 ml of reservoir solution containing 28% PEG 4000, 0.2 M sodium acetate, 0.1 M Tris-HCl, pH 8.4, at 8°C, 3 weeks, complexing by soaking of the crystals in a solution containing 2 mM D-captopril for 5 weeks, cryoprotection by 15% glycerol, X-ray diffraction structure determination and analysis at 1.5 A resolution
0.98 mg/ml purified mutant N152A in complex with inhibitor moxalactam in 1.7 M potassium phosphate, pH 8.7, 23°C, after microseeding with the wild-type enzyme in 1 M potassium phosphate, pH 8.7, vapor diffusion hanging drop method, serial dilutions, 5-7 days, X-ray diffraction structure determination and analysis at 1.83 A resolution
2.5-3 mg/ml purified recombinant enzyme in 10% PEG 8000, 0.05 M HEPES, pH 7.5, vapour diffusion sitting drop method, equilibration of 0.01 ml protein solution over a reservoir solution containing 20% PEG 8000, macro-seeding at 1.2-1.5 mg/ml, growth of prismatic crystals, X-ray diffraction structure determination and analysis at 1.5 A resolution, modeling
in complex with ([(benzylsulfonyl)amino]methyl)boronic acid, 4-([[(dihydroxyboranyl)methyl]sulfamoyl]methyl)benzoic acid, and 3-[(2R)-2-[(benzylsulfonyl)amino]-2-(dihydroxyboranyl)ethyl]benzoic acid, to 1.6, 1.8 and 1.6 A resolution, respectively. The sulfonamides have a highly distinct structure-activity relationship from the carboxamides, with high ligand efficiencies, and Ki values down to 25 nM and up to 23 times better for smaller analogs. Conversely, Ki values are 10 to 20 times worse for larger molecules than in the carboxamide congener series. X-ray crystal structures suggest that this altered structure-activity relationship results from the different geometry and polarity of the sulfonamide versus the carboxamide
purified recombinant enzyme, hanging drop vapor diffusion method, mixing of 9 mg/ml protein solution with crystallization solution containing 0.05 M HEPES, pH 7.5, and 15% PEG 8000, X-ray diffraction structure determination and analysis
hanging-drop vapour-diffusion. Two crystal forms are obtained from the same growth conditions. One is orthorhombic, with crystals that diffracted to better than 1.9 A, the other is tetragonal, with crystals that only diffracted to about 3.0 A. The orthorhombic crystal belongs to space group P2(1)2(1)2(1), with unit-cell parameters a = 46.54 A, b = 73.43 A, c = 84.56 A, while the tetragonal crystal has unit-cell parameters a = b = 73.72, c = 96.81 A
crystal structure of the complex of SHV-1 mutant D104E with beta-lactamse inhibitor protein BLIP, to 1.6 A resolution. Mutation D104E results in a 1000fold enhancement in binding affinity to BLIP, as it restores a salt bridge to BLIP. Mutation of a neighboring residue, BLIP E73M, results in salt bridge formation between SHV-1 D104 and BLIP K74 and a 400fold increase in binding affinity. BLIP F142 cooperatively stabilizes both interactions
purified recombinant enzyme, hanging-drop or sitting-drop vapor diffusion, mixing of 10 mg/ml protein in 10 mM Tris-HCl, pH 7.0, with reservoir solution containing of 20% PEG 8000, 100 mM sodium cacodylate, pH 6.5, and 0.2 M zinc acetate, to a finaal volume of 0.01 ml, equilibration against 0.5 ml reservoir solution, 1 month, 16°C, X-ray diffraction structure determination and analysis at 1.54 A resolution, modeling and molecular replacement
sitting-drop method, crystal structure of the OXA-48 carbapenemase is determined at pH 7.5 and at a resolution of 1.9 A. The enzyme shows a noncrystallographic pseudo 2-fold axis
BLaC is crystallized in the hanging drop vapor diffusion configuration over well conditions that include 0.1 M HEPES (pH 7.5) and 2 M NH4H2PO4. The final pH of the well solution is 4.1
enzyme in complex with inhibitor NXL104, hanging drop vapor diffusion, mixing of 12 mg/ml protein solution in a 1:1 ratio with well solution containing 0.1 M HEPES and 2 M NH4H2PO4, pH 4.1, 10°C, 4-5 days, microseeding, X-ray diffraction structure determination and analysis at 2.3 A resolution
purified recombinant detagged wild-type and mutant enzymes in complex with inhibitor tebipenem, hanging drop vapor diffusion, mixing of 12 mg/ml protein with 0.1 M HEPES and 2 M NH4H2PO4, pH 4.1, in a 1:1 ratio, 10°C, microseeding for the mutant enzyme, X-ray diffraction structure determination and analysis at 1.90 A and 1.75 A resolution
0.003 ml 10 mg/ml purified recombinant wild-type enzyme or mutant R234K, mixed with 0.001 ml of well solution containing 2 M ammonium sulfate, 50 mM MOPS pH 6.4, and 0.1 M acetate pH 4.5, respectively, 100 mM MgCl2, 1-2 weeks at room temperature, X-ray diffraction structure determination and analysis at 1.75 A resolution
as the native enzyme, with Cys221 oxidized, and with a sulfur atom bridging the two active-site zinc ions, to 1.9, 1.8 and 2.5 A resolution, respectively. Comparison with VIM-2 and VIM-4 structures suggests an explanation for the reduced catalytic efficiency of VIM-7 against cephalosporins with a positively charged cyclic substituent at the C3 position. Kinetic variations are attributed to substitutions in residues 6066, that form a loop adjacent to the active site previously implicated in substrate binding, and to the disruption of two hydrogen-bonding clusters through substitutions at positions 218 and 224
purified recombinant enzyme, sitting drop vapor diffusion method, mixxing of 0001 ml of 10 mg/mL VIM-2 protein with 0.001 ml of reservoir solution containing 0.2 M ammonium acetate, 0.1 mM zinc chloride, 0.1 M HEPES, pH 7.5, and 25% PEG 3350, X-ray diffraction tructure determination and analysis, molecular replacement
purified recombinant native and chloride-treated enzyme, from 1.8 M ammonium sulfate, 0.1 M MES, pH 6.5, 10 mM CoCl2, vapour diffusion method, X-ray diffraction structure determination and analysis at 2.0 A resolution, modeling
purified recombinant native and oxidized VIM-2, hanging drop vapour diffusion method, mixing 0.001 ml of 5.5 mg/ml of protein in 10 mM HEPES, pH 7.5, 0.2 M NaCl, and 1 mM DTT, with 0.001 ml of precipitant solution containing 30% PEG 8000, 0.2 M Na acetate, 0.1 M Na cacodylate/cacodylic acid, pH 6.5, and 0.01 mM ZnCl2, 20°C, 3-4 days, X-ray diffraction structure determination and analysis at 1.9-2.2 A resolution
purified recombinant enzyme, hanging drop vapor diffusion method, mixing of 0.0025 ml of 3.5mg/ml protein in , with 0.001 ml of crystallization solution containing 0.1 M HEPES in 1.5 M sodium citrate, pH 7.5, equilibration against 1.0 ml crystallization solution, 20°C, X-ray diffraction structure determination and analyysis at 2.2 A resolution, modeling
hanging-drop vapour diffusion method. Three-dimensional structures of D120A mutant and D120E mutant determined at 2.0 A and 3.0 A resolution, respectively
purified recombinant His-tagged enzyme, method screening, sitting drop vapour diffusion method, mixing of 0.001 ml protein solution with 0.001 ml reservoir solution containing 0.2 M ammonium sulfate, 0.1 M sodium acetate trihydrate, pH 5.3, 28% w/v PEG MME 2000, or 1.0 M lithium chloride, 0.1 M MES, pH 5.8, and 26% w/v PEG 6000, 1 week, 20°C, resulting in two different types of crystals: SMB-1a and SMB-1b, X-ray diffraction structure determination and analysis at 1.60-1.63 A resolution, molecular replacement and modeling
to 1.8 A resolution. The overall structure of ST1585 contains thirteen beta-strands and nine alpha-helices. The asymmetric unit of the crystal contains two monomers, and one cis peptide bond is observed between Pro181 and Val182. The overall structure is made up of an alpha-beta-beta-alpha structure. The two-metal ion-binding center is located at the external edge of the beta-beta sandwich, and two zinc ions are coordinated with conserved amino acid residues located in segments 2 to 5
recombinant His-tagged selenomethionyl-labeled EstSTR1 free and with bound PMSF, vapor batch crystallization method, mixing of 9 mg/ml protein and 1 mM PMSF with reservoir solution containing 25% w/v polyethylene glycol 3350, 100-mM 4-(2-hydroxyethyl)-1-piperazineethanesulfonic acid (HEPES) (pH 7.5), and 200-mM NaCl, 22°C, X-ray diffraction structure determination and analysis at 2.0 A resolution