1LUA
Structure of methylene-tetrahydromethanopterin dehydrogenase from Methylobacterium extorquens AM1 complexed with NADP
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | EMBL/DESY, HAMBURG BEAMLINE X11 |
| Synchrotron site | EMBL/DESY, HAMBURG |
| Beamline | X11 |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2000-09-30 |
| Detector | MARRESEARCH |
| Wavelength(s) | 0.81 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 75.900, 79.860, 154.290 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 29.130 - 1.900 |
| R-factor | 0.185 |
| Rwork | 0.185 |
| R-free | 0.22200 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | Methylene Tetrahydromethanopterin Dehydrogenase |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.310 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | CNS (1.0) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 2.000 |
| High resolution limit [Å] | 1.900 * | 1.900 |
| Rmerge | 0.091 | 0.270 |
| Number of reflections | 82475 | |
| <I/σ(I)> | 19 | 4.7 |
| Completeness [%] | 95.3 | 97.4 |
| Redundancy | 3.4 | 3.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 * | 4 * | PEG8000, MES, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 15 (mg/ml) | |
| 2 | 1 | drop | HEPES | 100 (mM) | pH7.5 |
| 3 | 1 | reservoir | PEG8000 | 17 (%) | |
| 4 | 1 | reservoir | MES | 50 (mM) | pH6.5 |
| 5 | 1 | reservoir | NADP+ | 5 (mM) |
