6WF5
Crystal structure of human Naa50 in complex with a truncated cofactor derived inhibitor (compound 2)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 17-ID |
| Synchrotron site | APS |
| Beamline | 17-ID |
| Temperature [K] | 93 |
| Detector technology | PIXEL |
| Collection date | 2017-04-20 |
| Detector | DECTRIS PILATUS3 S 6M |
| Wavelength(s) | 1.0 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 50.937, 52.339, 64.123 |
| Unit cell angles | 90.00, 97.38, 90.00 |
Refinement procedure
| Resolution | 50.520 - 2.040 |
| R-factor | 0.224 |
| Rwork | 0.222 |
| R-free | 0.27400 |
| Structure solution method | FOURIER SYNTHESIS |
| Starting model (for MR) | 6wf3 |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.130 |
| Data reduction software | XDS |
| Data scaling software | autoPROC |
| Phasing software | BUSTER |
| Refinement software | BUSTER (2.11.7) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 63.590 | 2.150 |
| High resolution limit [Å] | 2.040 | 2.040 |
| Rmerge | 0.126 | 0.723 |
| Number of reflections | 21247 | 3080 |
| <I/σ(I)> | 7.9 | |
| Completeness [%] | 98.8 | 98.6 |
| Redundancy | 3.3 | 3.3 |
| CC(1/2) | 0.991 | 0.667 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 286.15 | Co-crystallization: Naa50 apo protein (14.3 mg/ml) was incubated with compound 2 in a 1:3 molar ratio on ice for 60 min. Reservoir solution containing 0.2 M ammonium sulfate and 30% (w/v) PEG 3K/4K was mixed 1:1 with protein:ligand complex |
