2WUU
Structure of N-myristoyltransferase from L. donovani
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID23-1 |
| Synchrotron site | ESRF |
| Beamline | ID23-1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2009-04-19 |
| Detector | ADSC CCD |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 45.970, 90.131, 92.355 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 40.000 - 1.420 |
| R-factor | 0.14866 |
| Rwork | 0.146 |
| R-free | 0.19055 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1nmt |
| RMSD bond length | 0.023 |
| RMSD bond angle | 2.077 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.5.0102) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 40.000 | 1.460 |
| High resolution limit [Å] | 1.420 | 1.420 |
| Rmerge | 0.100 | 0.360 |
| Number of reflections | 68150 | |
| <I/σ(I)> | 10.8 | 3 |
| Completeness [%] | 98.1 | 78.8 |
| Redundancy | 7.4 | 2.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 4 | 0.6 M LICL, 0.05 M NACITRATE PH 4.0, 20% (W/V) PEG 6000 |
