5FTW
Crystal structure of glutamate O-methyltransferase in complex with S- adenosyl-L-homocysteine (SAH) from Bacillus subtilis
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | BRUKER AXS MICROSTAR-H |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2013-07-30 |
Detector | MARRESEARCH |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 41.580, 72.870, 81.860 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 36.460 - 1.800 |
R-factor | 0.17948 |
Rwork | 0.176 |
R-free | 0.23699 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1bc5 |
RMSD bond length | 0.017 |
RMSD bond angle | 2.150 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | MOLREP |
Refinement software | REFMAC (5.7.0029) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 41.580 | 1.890 |
High resolution limit [Å] | 1.790 | 1.790 |
Rmerge | 0.150 | 0.600 |
Number of reflections | 23011 | |
<I/σ(I)> | 8.1 | 2.3 |
Completeness [%] | 96.1 | 83.4 |
Redundancy | 4.7 | 4.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 0.2 M AMMONIUM SULFATE, 0.1 M SODIUM ACETATE TRIHYDRATE |