4KVM
The NatA (Naa10p/Naa15p) amino-terminal acetyltransferase complex bound to a bisubstrate analog
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSLS BEAMLINE X25 |
| Synchrotron site | NSLS |
| Beamline | X25 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2012-10-03 |
| Detector | PSI PILATUS 6M |
| Wavelength(s) | 0.9795 |
| Spacegroup name | P 1 |
| Unit cell lengths | 81.439, 119.381, 134.063 |
| Unit cell angles | 80.20, 76.60, 70.42 |
Refinement procedure
| Resolution | 49.590 - 2.597 |
| R-factor | 0.2235 |
| Rwork | 0.222 |
| R-free | 0.25960 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4kvx |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.166 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | PHENIX ((phenix.refine: 1.7.3_928)) |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 50.000 |
| High resolution limit [Å] | 2.600 |
| Number of reflections | 137534 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 298 | Protein Buffer: 25 mM Hepes, pH 7.0, 200 mM NaCl, 1 mM TCEP Crystallization buffer: 100 mM Hepes, pH 7.0, 10% Peg 4000, 10% isopropanol, VAPOR DIFFUSION, HANGING DROP, temperature 298K |






