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 |
