6GNH
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 ID14-1 |
| Synchrotron site | ESRF |
| Beamline | ID14-1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2009-06-12 |
| Detector | ADSC QUANTUM 210 |
| Wavelength(s) | 0.933 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 48.613, 90.990, 53.561 |
| Unit cell angles | 90.00, 114.61, 90.00 |
Refinement procedure
| Resolution | 38.710 - 1.890 |
| R-factor | 0.1718 |
| Rwork | 0.169 |
| R-free | 0.23340 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2wsa |
| RMSD bond length | 0.019 |
| RMSD bond angle | 1.931 |
| 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 | 1.900 |
| High resolution limit [Å] | 1.890 | 1.890 |
| Rmerge | 0.067 | |
| Number of reflections | 28979 | |
| <I/σ(I)> | 15 | |
| Completeness [%] | 86.0 | 65 |
| Redundancy | 3 | 2.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 5.6 | 291 | 26%PEG1500,0.2M NACL, 0.1M NACACODYLATE, PH 5.6 |
