3SXT
Crystal Structure of the Quinol Form of Methylamine Dehydrogenase in Complex with the Diferrous Form of MauG
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 23-ID-B |
Synchrotron site | APS |
Beamline | 23-ID-B |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2011-06-29 |
Detector | MARMOSAIC 300 mm CCD |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 62.639, 135.664, 111.557 |
Unit cell angles | 90.00, 97.37, 90.00 |
Refinement procedure
Resolution | 35.010 - 1.810 |
R-factor | 0.147 |
Rwork | 0.145 |
R-free | 0.18700 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3l4m |
RMSD bond length | 0.026 |
RMSD bond angle | 2.092 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | REFMAC (5.5.0109) |
Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.840 |
High resolution limit [Å] | 1.810 | 1.810 |
Number of reflections | 164390 | |
<I/σ(I)> | 16.7 | 2.3 |
Completeness [%] | 98.3 | 80.9 |
Redundancy | 6.5 | 2.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 6.4 | 293 | Drops contained 1uL protein with 3uL reservoir solution. WT-MauG and MADH were each reduced in an anaerobic glove box prior to preparing the protein mixture for crystallization. Protein mixture: 100uM reduced WT-MauG and 50uM reduced MADH in 10mM potassium phosphate pH7.5 with 2mM sodium dithionite. Reservoir solution contained: 22% w/v PEG 8000, 0.1M sodium acetate, 0.1M MES pH 6.4 and 2mM sodium dithionite. Crystallization was carried out in an anaerobic glove box at ambient temperature., VAPOR DIFFUSION, HANGING DROP, temperature 293K |