3QFH
2.05 Angstrom Resolution Crystal Structure of Epidermin Leader Peptide Processing Serine Protease (EpiP) from Staphylococcus aureus.
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 | 2010-11-14 |
| Detector | MARMOSAIC 225 mm CCD |
| Wavelength(s) | 0.97872 |
| Spacegroup name | P 1 |
| Unit cell lengths | 85.505, 94.696, 122.999 |
| Unit cell angles | 89.98, 90.37, 116.79 |
Refinement procedure
| Resolution | 29.690 - 2.050 |
| R-factor | 0.1718 |
| Rwork | 0.170 |
| R-free | 0.21596 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1thm |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.353 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-3000 |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.5.0102) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 2.090 |
| High resolution limit [Å] | 2.050 | 2.050 |
| Rmerge | 0.047 | 0.354 |
| Number of reflections | 219399 | |
| <I/σ(I)> | 15 | 2.1 |
| Completeness [%] | 97.9 | 97 |
| Redundancy | 2 | 2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 5.5 | 295 | Protein: 7mg/mL, ?M Sodium cloride, Tris-HCl (pH 8.3), Screen: GCSG+ (H9), 0.2M Lithium sulfate, 0.1M Bis-Tris pH 5.5, 25% (w/v) PEG 3350, VAPOR DIFFUSION, SITTING DROP, temperature 295K |
