6PAV
Structure of Human NMT1 with products CoA and myristoyl-lysine peptide with acetylated N-terminus
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 | 2019-04-05 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 0.97918 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 92.361, 58.217, 154.035 |
| Unit cell angles | 90.00, 90.66, 90.00 |
Refinement procedure
| Resolution | 77.012 - 2.520 |
| R-factor | 0.2663 |
| Rwork | 0.265 |
| R-free | 0.28040 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.013 |
| RMSD bond angle | 1.575 |
| 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] | 77.012 | 2.610 |
| High resolution limit [Å] | 2.520 | 2.520 |
| Rmerge | 0.305 | 1.196 |
| Number of reflections | 27918 | 2722 |
| <I/σ(I)> | 4.98 | |
| Completeness [%] | 98.5 | 97.21 |
| Redundancy | 3.8 | 3.6 |
| CC(1/2) | 0.919 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 293 | 7.5 mg/mL in 25 mM Tris-HCl pH 7.5, 120 mM NaCl, co-crystallized in the presence of 0.3 mM myristoyl-CoA and 0.3 mM AcKVLSKIF using a well solution of 18% PEG 8000, 100 mM NaCl, 100 mM |
