1G72
CATALYTIC MECHANISM OF QUINOPROTEIN METHANOL DEHYDROGENASE: A THEORETICAL AND X-RAY CRYSTALLOGRAPHIC INVESTIGATION
Replaces: 1B2NExperimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | PHOTON FACTORY BEAMLINE BL-6B |
Synchrotron site | Photon Factory |
Beamline | BL-6B |
Temperature [K] | 277 |
Detector technology | DIFFRACTOMETER |
Collection date | 1995-11-01 |
Detector | WEISSENBERG |
Wavelength(s) | 1.0 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 98.115, 69.744, 109.838 |
Unit cell angles | 90.00, 110.29, 90.00 |
Refinement procedure
Resolution | 100.000 - 1.900 |
R-factor | 0.1605 |
Rwork | 0.161 |
R-free | 0.18980 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4aah |
RMSD bond length | 0.005 |
RMSD bond angle | 25.100 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | MERLOT |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 40.000 | 1.970 |
High resolution limit [Å] | 1.900 | 1.900 |
Rmerge | 0.091 | 0.810 |
Number of reflections | 108348 | |
<I/σ(I)> | 15.5 | 1.9 |
Completeness [%] | 98.6 | 95.6 |
Redundancy | 5 | 4.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion * | 9.2 * | 295 | Oubrie, A., (1999) J.Mol.Biol., 289, 319. * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 5 (mg/ml) | |
2 | 1 | drop | PQQ | 0.1 (mM) | |
3 | 1 | drop | PEG6000 | 8 (%(w/v)) | |
4 | 1 | drop | Tris-glycine | 50 (mM) | |
5 | 1 | reservoir | PEG6000 | 20-23 (%(w/v)) | |
6 | 1 | reservoir | 120 (mM) | ||
7 | 1 | reservoir | 3 (mM) | ||
8 | 1 | reservoir | Tris-glycine | 50 (mM) |