4RFB
1.93 Angstrom Crystal Structure of Superantigen-like Protein from Staphylococcus aureus in Complex with Sialyl-Lewis X.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 21-ID-D |
| Synchrotron site | APS |
| Beamline | 21-ID-D |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2014-03-20 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 0.97875 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 42.640, 108.199, 167.655 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 28.830 - 1.930 |
| R-factor | 0.17106 |
| Rwork | 0.169 |
| R-free | 0.21829 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3v05 |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.637 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-3000 |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.7.0032) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 1.960 |
| High resolution limit [Å] | 1.930 | 1.930 |
| Rmerge | 0.074 | 0.552 |
| Number of reflections | 61498 | |
| <I/σ(I)> | 19.3 | 3 |
| Completeness [%] | 99.7 | 100 |
| Redundancy | 4.9 | 4.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 295 | Protein: 7.4mG/mL, 0.25M Sodium chloride, 0.01M Tris-HCl (pH 8.3); Screen: PEGsII (F12), 0.8M Lithium chloride, 0.1M Tris (pH 8.5), 32% (w/v) PEG 4000, VAPOR DIFFUSION, SITTING DROP, temperature 295K |
