4Q29
Ensemble Refinement of plu4264 protein from Photorhabdus luminescens
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 19-ID |
| Synchrotron site | APS |
| Beamline | 19-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2012-10-22 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.98 |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 55.738, 147.687, 83.843 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 24.898 - 1.349 |
| R-factor | 0.1268 |
| Rwork | 0.126 |
| R-free | 0.15530 |
| Structure solution method | SAD |
| RMSD bond length | 0.020 |
| RMSD bond angle | 2.097 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-3000 |
| Phasing software | SHELX |
| Refinement software | PHENIX (1.8.4_1496) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 1.370 |
| High resolution limit [Å] | 1.349 | 1.350 |
| Number of reflections | 76134 | |
| Completeness [%] | 99.8 | 99.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 289 | 0.2 M Li2SO4, 0.1 M Tris/HCl 8.5, 25% PEG400, VAPOR DIFFUSION, SITTING DROP, temperature 289K |
