8FBQ
Crystal structure of Plasmodium vivax glycylpeptide N-tetradecanoyltransferase (N-myristoyltransferase, NMT) bound to myristoyl-CoA and inhibitor 12b
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ALS BEAMLINE 8.2.2 |
| Synchrotron site | ALS |
| Beamline | 8.2.2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2022-05-21 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 1.00000 |
| Spacegroup name | P 43 21 2 |
| Unit cell lengths | 91.930, 91.930, 101.286 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 45.970 - 1.650 |
| R-factor | 0.1375 |
| Rwork | 0.136 |
| R-free | 0.16480 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 6nxg |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.085 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.19.1-4122-000) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 1.680 |
| High resolution limit [Å] | 1.650 | 4.480 | 1.650 |
| Rmerge | 0.116 | 0.032 | 0.889 |
| Rmeas | 0.120 | 0.033 | 0.924 |
| Rpim | 0.032 | 0.009 | 0.246 |
| Total number of observations | 751443 | ||
| Number of reflections | 52868 | 2903 | 2577 |
| <I/σ(I)> | 5.3 | ||
| Completeness [%] | 100.0 | 100 | 100 |
| Redundancy | 14.2 | 13.6 | 13.4 |
| CC(1/2) | 0.999 | 0.903 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 4.5 | 295 | JCSG+ condition A1: 0.2 M lithium sulfate, 0.1 M sodium acetate, 50% PEG 400, pH 4.5 |
