EC Number   |
Reference |
|---|
    1.5.98.1 | crystallization trials are performed with the hanging drop vapor diffusion method using a sparse matrix crystallization kit under anaerobic and red light conditions, determination the structures of the Mtd-5,10-methylenetetrahydromethanopterin-, Mtd-5,10-methenyltetrahydromethanopterin- and the Mtd-5,10-methenyltetrahydromethanopterin-F420H2 complexes at 2.1, 2.0, and 1.8 A resolution, both substrate and cofactor bind in a face to face arrangement to an active site cleft, thereby ensuring a direct hydride transfer between their C14a and C5 atoms |
696301 |
| 1.5.98.1 | hanging drop vapour diffusion method, crystal structure of the enzyme in complex with cytochrome F420 at 2.6 A resolution |
677003 |
| 1.5.98.1 | purified recombinant selenomethionine-labeled enzyme, hanging drop vapour diffusion method, 0.001 ml protein solution containing 12 mg/ml enzyme and 10 mM MOPS-KOH, pH 7.0, mixed with 0.001 ml reservoir solution containing 13% v/v 2-methyl-2,4-pentanediol, 0.1 M sodium phosphate, pH 8.0, and 0.2 M magnesium acetate, X-ray diffraction structure determination and analysis at 1.54 A resolution by single wavelength anomalous dispersion method, or at 2.4 A resolution by multiwavelength anomalous dispersion method |
654077 |
| 1.5.98.1 | selenomethionine-labeled enzyme: X-ray diffraction structure determination and analysis at 1.54 A resolution, atomic displacement B factor pattern, native enzyme: X-ray diffraction structure determination and analysis at 2.0-2.4 A resolution, the native enzyme shows a crystallographic superstructure of the selenomethionine-labeled enzyme |
654120 |
| 1.5.98.1 | the selenomethionine-labelled form of the enzyme is structurally characterized at 1.54 A resolution |
728130 |
