4HS7
2.6 Angstrom Structure of the Extracellular Solute-binding Protein from Staphylococcus aureus in complex with PEG.
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 | 2012-10-18 |
| Detector | MARMOSAIC 225 mm CCD |
| Wavelength(s) | 0.97872 |
| Spacegroup name | P 65 |
| Unit cell lengths | 101.863, 101.863, 191.341 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 29.990 - 2.600 |
| R-factor | 0.17003 |
| Rwork | 0.167 |
| R-free | 0.21933 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2zyo |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.370 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-3000 |
| Phasing software | BALBES |
| Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 2.640 |
| High resolution limit [Å] | 2.600 | 2.600 |
| Rmerge | 0.090 | 0.644 |
| Number of reflections | 34117 | |
| <I/σ(I)> | 17.7 | 3 |
| Completeness [%] | 98.8 | 99.6 |
| Redundancy | 5.4 | 5.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8.3 | 295 | Protein: 7.4mg/mL, 0.25M Sodium cloride, 0.01M Tris-HCl pH 8.3; Screen: JCSG+ (B12), 0.2M tri-Potassium citrate pH 8.3, 20% (w/v) PEG 3350, VAPOR DIFFUSION, SITTING DROP, temperature 295K |
