4QVR
2.3 Angstrom Crystal Structure of Hypothetical Protein FTT1539c from Francisella tularensis.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 21-ID-F |
| Synchrotron site | APS |
| Beamline | 21-ID-F |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2014-06-30 |
| Detector | MARMOSAIC 225 mm CCD |
| Wavelength(s) | 0.97872 |
| Spacegroup name | P 1 |
| Unit cell lengths | 36.006, 47.424, 55.115 |
| Unit cell angles | 91.00, 102.19, 99.50 |
Refinement procedure
| Resolution | 26.640 - 2.300 |
| R-factor | 0.17621 |
| Rwork | 0.174 |
| R-free | 0.22445 |
| Structure solution method | SAD |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.437 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-3000 |
| Phasing software | PHENIX |
| Refinement software | REFMAC (5.7.0032) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 2.340 |
| High resolution limit [Å] | 2.300 | 2.300 |
| Rmerge | 0.073 | 0.564 |
| Number of reflections | 15653 | |
| <I/σ(I)> | 33.1 | 3.4 |
| Completeness [%] | 98.5 | 97.7 |
| Redundancy | 5.9 | 6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7 | 295 | Protein: 6.9 mg/ml, 0.25 M Sodium chloride, 0.01 M Tris-HCL buffer pH(8.3), 5mM BME; Screen: PACT (D4), 0.1M MMT buffer (pH 7.0), 25%(w/v) PEG 1500., VAPOR DIFFUSION, SITTING DROP, temperature 295K |
