6PAU
Structure of Human NMT2 with myristoyl-lysine peptide and CoA products
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 24-ID-E |
| Synchrotron site | APS |
| Beamline | 24-ID-E |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2019-03-21 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 0.97918 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 63.162, 46.350, 74.395 |
| Unit cell angles | 90.00, 114.25, 90.00 |
Refinement procedure
| Resolution | 67.831 - 1.930 |
| R-factor | 0.1984 |
| Rwork | 0.197 |
| R-free | 0.21770 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4c2x |
| RMSD bond length | 0.007 |
| RMSD bond angle | 0.877 |
| Data reduction software | XDS |
| Data scaling software | Aimless |
| Phasing software | PHASER |
| Refinement software | PHENIX ((1.13_2998: ???)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 57.590 | 1.999 |
| High resolution limit [Å] | 1.930 | 1.930 |
| Rmerge | 0.101 | 1.066 |
| Rmeas | 0.112 | |
| Number of reflections | 154166 | 15911 |
| <I/σ(I)> | 11.35 | 1.54 |
| Completeness [%] | 99.5 | 99.56 |
| Redundancy | 5.2 | 5.3 |
| CC(1/2) | 0.998 | 0.646 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 293 | 8 mg/mL protein in a buffer of 25 mM Tris-HCl pH 7.5, 120 mM NaCl, 1 mM DTT, 1 mM MgCl2, mixed 1:1 with well solution of 22% PEG 8000, 0.1 M Bis-Tris pH 6.5 |
