6GNS
Crystal Structure of Leishmania major N-Myristoyltransferase (NMT) With Bound Myristoyl-CoA and an Azepanyl Phenyl Benzylsulphonamide Ligand
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID29 |
| Synchrotron site | ESRF |
| Beamline | ID29 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2010-02-13 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.98 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 48.426, 90.437, 52.982 |
| Unit cell angles | 90.00, 114.76, 90.00 |
Refinement procedure
| Resolution | 43.970 - 1.800 |
| R-factor | 0.1711 |
| Rwork | 0.169 |
| R-free | 0.21810 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2wsa |
| RMSD bond length | 0.018 |
| RMSD bond angle | 1.927 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.8.0049) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.860 |
| High resolution limit [Å] | 1.800 | 1.800 |
| Rmerge | 0.082 | 0.340 |
| Number of reflections | 37104 | |
| <I/σ(I)> | 13 | 2.1 |
| Completeness [%] | 96.0 | 84 |
| Redundancy | 3.3 | 2.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5.6 | 291 | 26%PEG1500,0.2M NACL, 0.1M NACACODYLATE, PH 5.6 |
