3TFY
Naa50p amino-terminal acetyltransferase bound to substrate peptide fragment and CoA
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSLS BEAMLINE X6A |
| Synchrotron site | NSLS |
| Beamline | X6A |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2010-06-10 |
| Detector | ADSC QUANTUM 270 |
| Wavelength(s) | 1.1271 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 48.299, 104.103, 68.247 |
| Unit cell angles | 90.00, 106.29, 90.00 |
Refinement procedure
| Resolution | 33.659 - 2.750 |
| R-factor | 0.1935 |
| Rwork | 0.190 |
| R-free | 0.25370 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2PSW (cofactor and solvent removed) |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.596 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | PHENIX ((phenix.refine: 1.6_289)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.800 |
| High resolution limit [Å] | 2.750 | 2.750 |
| Number of reflections | 16856 | |
| <I/σ(I)> | 10.2 | 2.1 |
| Completeness [%] | 98.9 | 93.2 |
| Redundancy | 3.6 | 3.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5 | 273 | well solution: 16% PEG 8000, 20% glycerol, 40mM potassium phosphate (monobasic), pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 273K |
