3SST
Engineered low-affinity halide-binding protein derived from YFP: chloride complex
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 22-ID |
| Synchrotron site | APS |
| Beamline | 22-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2009-12-17 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 1.0000 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 51.494, 62.688, 69.764 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 34.882 - 1.403 |
| R-factor | 0.1621 |
| Rwork | 0.161 |
| R-free | 0.18220 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2o24 |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.488 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.7.1_743) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 41.430 | 50.000 | 1.420 |
| High resolution limit [Å] | 1.403 | 3.800 | 1.400 |
| Rmerge | 0.075 | 0.054 | 0.490 |
| Number of reflections | 39190 | ||
| <I/σ(I)> | 13.3 | ||
| Completeness [%] | 87.4 | 75.1 | 86.5 |
| Redundancy | 4.8 | 5.1 | 3.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5.6 | 290 | 14% PEG4000, 50 mM sodium acetate, pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 290K |
