3QTB
Structure of the universal stress protein from Archaeoglobus fulgidus in complex with dAMP
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 21-ID-G |
| Synchrotron site | APS |
| Beamline | 21-ID-G |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2008-08-22 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 0.9786 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 109.607, 42.655, 61.289 |
| Unit cell angles | 90.00, 116.82, 90.00 |
Refinement procedure
| Resolution | 50.000 - 2.100 |
| R-factor | 0.2017 |
| Rwork | 0.200 |
| R-free | 0.23747 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3DLO |
| RMSD bond length | 0.014 |
| RMSD bond angle | 1.425 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-3000 |
| Phasing software | HKL-3000 |
| Refinement software | REFMAC (5.6.0070) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.140 |
| High resolution limit [Å] | 2.100 | 2.100 |
| Rmerge | 0.070 | 0.405 |
| Number of reflections | 14965 | |
| <I/σ(I)> | 21.5 | 2.5 |
| Completeness [%] | 98.8 | 99.6 |
| Redundancy | 2.5 | 2.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5.5 | 293 | 0.2M ammonium sulfate, 0.1M BIS-TRIS pH 5.5, 25%w/v polyethylene glycol, 3350, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
