1W6F
Arylamine N-acetyltransferase from Mycobacterium smegmatis with the anti-tubercular drug isoniazid bound in the active site.
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID14-1 |
Synchrotron site | ESRF |
Beamline | ID14-1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2003-11-27 |
Detector | ADSC CCD |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 101.208, 106.039, 140.362 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 84.520 - 2.100 |
R-factor | 0.182 |
Rwork | 0.180 |
R-free | 0.21900 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1GX3 CHAIN A |
RMSD bond length | 0.019 |
RMSD bond angle | 1.702 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | MOLREP |
Refinement software | REFMAC (5.1.24) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 31.620 | 2.110 |
High resolution limit [Å] | 1.390 | 2.000 |
Rmerge | 0.120 | 0.610 |
Number of reflections | 84858 | |
<I/σ(I)> | 5.17 | 1.16 |
Completeness [%] | 92.2 | 92.1 |
Redundancy | 3.34 | 3.62 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 6.5 | 0.2M AMMONIUM SULPHATE, 0.1M MES PH 6.5, 30% PEG MME 5000 |