6F56
Mutant of Human N-myristoyltransferase with bound myristoyl-CoA
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE MASSIF-1 |
| Synchrotron site | ESRF |
| Beamline | MASSIF-1 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2017-09-29 |
| Detector | DECTRIS PILATUS3 2M |
| Wavelength(s) | 0.966 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 58.190, 159.130, 174.990 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 87.495 - 1.940 |
| R-factor | 0.201532698232 |
| Rwork | 0.200 |
| R-free | 0.23944 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4c2y |
| RMSD bond length | 0.003 |
| RMSD bond angle | 0.691 |
| Data reduction software | XDS (BUILT=20170615) |
| Data scaling software | XSCALE (BUILT=20170615) |
| Phasing software | PHASER (2.8.0) |
| Refinement software | PHENIX (1.12_2829) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 87.495 | 1.974 |
| High resolution limit [Å] | 1.940 | 1.940 |
| Rmerge | 0.100 | 0.839 |
| Rmeas | 0.119 | 1.003 |
| Rpim | 0.063 | 0.541 |
| Number of reflections | 112254 | 4257 |
| <I/σ(I)> | 11.3 | 2.1 |
| Completeness [%] | 92.8 | 72.2 |
| Redundancy | 6.5 | 5.7 |
| CC(1/2) | 0.998 | 0.801 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 4.6 | 293.15 | PEG 4000 22 % Sodium citrate 0.1 M Glycerol 2.5 % |
