4NF1
Structure of N-acetyltransferase domain of X. fastidiosa NAGS/K without his-tag
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 | 2013-07-17 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 1.0 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 63.871, 123.350, 76.659 |
| Unit cell angles | 90.00, 107.62, 90.00 |
Refinement procedure
| Resolution | 34.073 - 1.399 |
| R-factor | 0.1794 |
| Rwork | 0.179 |
| R-free | 0.19930 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4nex |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.082 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER (2.5.3) |
| Refinement software | PHENIX (1.9_1692) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 40.000 | 1.420 |
| High resolution limit [Å] | 1.399 | 1.399 |
| Rmerge | 0.084 | 0.900 |
| Number of reflections | 209796 | |
| <I/σ(I)> | 32.9 | 2 |
| Completeness [%] | 94.5 | 96.5 |
| Redundancy | 7.1 | 6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 291 | 0.2 M Li2SO4, 0.1 M Tris pH 8.5 25% PEG3350, VAPOR DIFFUSION, SITTING DROP, temperature 191K, temperature 291K |
