4NEX
Structure of the N-acetyltransferase domain of X. fastidiosa NAGS/K
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 22-ID |
| Synchrotron site | APS |
| Beamline | 22-ID |
| Temperature [K] | 298 |
| Detector technology | CCD |
| Collection date | 2013-06-16 |
| Detector | MARMOSAIC 300 mm CCD |
| Spacegroup name | P 41 21 2 |
| Unit cell lengths | 51.718, 51.718, 242.309 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 39.330 - 1.696 |
| R-factor | 0.191 |
| Rwork | 0.189 |
| R-free | 0.21900 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3s6h |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.099 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER (2.5.3) |
| Refinement software | PHENIX (1.8.2_1309) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 40.000 | 1.730 |
| High resolution limit [Å] | 1.696 | 1.696 |
| Rmerge | 0.079 | 0.690 |
| Number of reflections | 37347 | |
| <I/σ(I)> | 55.8 | 3.4 |
| Completeness [%] | 98.4 | 97.2 |
| Redundancy | 13 | 10.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 6.5 | 291 | 0.2 M Li2SO4, 0.1 M Tris, pH 6.5, 25% PEG3350 , VAPOR DIFFUSION, SITTING DROP, temperature 291K |
