3T41
1.95 Angstrom Resolution Crystal Structure of Epidermin Leader Peptide Processing Serine Protease (EpiP) S393A Mutant from Staphylococcus aureus
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 21-ID-G |
| Synchrotron site | APS |
| Beamline | 21-ID-G |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2011-04-21 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 0.97856 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 71.234, 68.473, 97.723 |
| Unit cell angles | 90.00, 91.66, 90.00 |
Refinement procedure
| Resolution | 29.940 - 1.950 |
| R-factor | 0.16749 |
| Rwork | 0.166 |
| R-free | 0.19477 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3qfh |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.377 |
| 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 | 1.980 |
| High resolution limit [Å] | 1.950 | 1.950 |
| Rmerge | 0.045 | 0.473 |
| Number of reflections | 67885 | |
| <I/σ(I)> | 25.5 | 3 |
| Completeness [%] | 98.0 | 97.8 |
| Redundancy | 3.8 | 3.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8 | 295 | Protein solution: 7.8 mG/mL, 0.25M Sodium chloride, 0.01M Tris HCl (pH 8.3), Screen solution: PACT (D11), 0.2M Calcium chloride, 0.1M Tris (pH 8.0), 20% w/v PEG 6000, VAPOR DIFFUSION, SITTING DROP, temperature 295K |
