4A95
Plasmodium vivax N-myristoyltransferase with quinoline inhibitor
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID14-4 |
Synchrotron site | ESRF |
Beamline | ID14-4 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2011-03-07 |
Detector | ADSC CCD |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 57.490, 121.560, 179.010 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 72.080 - 1.550 |
R-factor | 0.18897 |
Rwork | 0.186 |
R-free | 0.23596 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | PVNMT |
RMSD bond length | 0.024 |
RMSD bond angle | 2.083 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | MOLREP |
Refinement software | REFMAC (5.6.0116) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 72.000 | 1.590 |
High resolution limit [Å] | 1.550 | 1.550 |
Rmerge | 0.090 | 0.350 |
Number of reflections | 154218 | |
<I/σ(I)> | 15.6 | 2.3 |
Completeness [%] | 85.2 | 46.6 |
Redundancy | 8.1 | 2.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 6 | 0.2 M AS, 25% PEG 3350, 0.1 M BIS-TRIS PH 6.0 |