EC Number   |
|---|
   1.1.2.7 | Ba2+-containing MDH active site model to investigate the two proposed addition-elimination and hydride-transfer methanol oxidation mechanisms |
| 1.1.2.7 | crystal structure analysis |
| 1.1.2.7 | crystal structure determination |
| 1.1.2.7 | enzyme or cytochrome cL, hanging drop vapour diffusion method, 16°C, 0.001 ml of 20 mg/mL enzyme or cofactor in 40 mM Tris-HCl buffer, pH 7.5, is mixed with an equal volume of precipitant colution containing 0.2 M potassium thiocyanate and 20% PEG 3350 for the enzyme crystallization, and 2 mM ZnSO4, 20% PEG 10000, and 100 mM HEPES, pH 7.3, for the crystallization of Cyt cL, 1 week to 1 month, X-ray diffraction structure determination and analysis at 1.98-2.5 A resolution |
| 1.1.2.7 | hanging-drop vapor diffusion method, X-ray structures of methanol dehydrogenase (Hd-MDH) and cytochrome cL at 2.5 A and 2.0 A resolution, respectively. Docking simulation between the coupled cytochrome cL molecules and the heterotetrameric methanol dehydrogenase |
| 1.1.2.7 | purified enzyme, 5 mg/mL protein in 50 mM Tris-HCl, pH 8.25, and 13.5% PEG 8000, mixed with crystallization solution containing 1 and 50 mM methanol resulting in crystal forms A, B or C with or without incorporated methanol or ethanool, 20°C, X--ray diffraction structure determination and analysis at 1.5-3.0 A resolution, molecular modeling |
| 1.1.2.7 | purified heme c containing CytcL from Methylophaga aminisulfidivorans (Ma-CytcL), hanging drop vapor diffusion method, mixing of 0.001 ml of 12 mg/ml protein solution containing 800 mM sodium phosphate monobasic, 100 mM HEPES/sodium hydroxide, pH 7.5, with 0.001 ml of reservoir solution containing 0.2 M lithium sulfate monohydrate, 0.1 M bis-Tris, pH 5.5, and 25% PEG 3350, at 20°C for 21 days, X-ray diffraction structure determination analysis at 2.13 A resolution, molecular replacement using the structures of cytochrome cL from Methylobacterium extorquens (Me-CytcL, PDB ID 2C8S) and Hyphomicrobium denitrificans (Hd-CytcL, PDB ID 2D0W) as model structures, modeling |
| 1.1.2.7 | purified holoenzyme, hanging-drop vapour-diffusion method, 3 ml of 15 mg/ml protein solution, 20 mM Tris buffer, pH 8.0, are placed on siliconized cover slips and mixed with an equal volume of well solution, the cover slip is sealed with high-vacuum grease over a 1 ml well containing 20% PEG 8000, pH 9.0, large crystals after two weeks, X-ray diffraction structure determination and analysis at 1.2 A resolution, modeling |
| 1.1.2.7 | purified native enzyme, hanging drop vapour diffusion method, 8 mg/ml protein in 25 mM Tris-HCl, pH 8.0, mixed with 0.1 M sodium cacodylate pH 6.5, 0.2 M magnesium acetate tetrahydrate and 10% v/v PEG 8000, 20°C, macrocrystals are soaked for 30 s in cryosolution consisting of crystallization solution with 20% v/v glycerol, X-ray diffraction structure determination and analysis at 1.7 A reolution, molecular replacement |
| 1.1.2.7 | purified recombinant MxaJ(residues 12-281), hanging drop vapor diffusion method, mixing of 0.001 ml of 10 mg/ml protein solution with 0.001 ml of reservoir solution containing 0.1 M Tris-HCl, pH 8.5, 0.2 M sodium bromide, 20% w/v PEG 3350, and 10% w/v glycerol, at 20°C, X-ray diffraction structure determination and analysis at 1.92 A resolution, modeling |
