4RGT
2.0 Angstrom Crystal Structure of Superantigen-like Protein from Staphylococcus aureus in Complex with 3-N-Acetylneuraminyl-N-acetyllactosamine.
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 | 2014-08-25 |
| Detector | MARMOSAIC 225 mm CCD |
| Wavelength(s) | 0.97872 |
| Spacegroup name | P 64 |
| Unit cell lengths | 141.832, 141.832, 41.991 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 29.310 - 2.000 |
| R-factor | 0.20028 |
| Rwork | 0.198 |
| R-free | 0.24704 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3v05 |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.606 |
| 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 | 2.030 |
| High resolution limit [Å] | 2.000 | 2.000 |
| Rmerge | 0.063 | 0.627 |
| Number of reflections | 32916 | |
| <I/σ(I)> | 25.8 | 2.8 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 6 | 6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7 | 295 | Protein: 7.4mG/mL, 0.25M Sodium chloride, 0.01M Tris-HCl (pH 8.3); Screen: Classics II (D3), 0.1M HEPES (pH 7.0), 30% (v/v) Jeffamine ED-2001., VAPOR DIFFUSION, SITTING DROP, temperature 295K |
