3QFG
Structure of a putative lipoprotein from Staphylococcus aureus subsp. aureus NCTC 8325
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 | 2010-12-06 |
| Detector | MARMOSAIC 225 mm CCD |
| Wavelength(s) | 0.97872 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 52.346, 60.739, 114.385 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 57.170 - 3.080 |
| R-factor | 0.23482 |
| Rwork | 0.233 |
| R-free | 0.27594 |
| Structure solution method | SAD |
| RMSD bond length | 0.021 |
| RMSD bond angle | 1.873 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-3000 |
| Phasing software | HKL-3000 |
| Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 57.170 | 3.150 |
| High resolution limit [Å] | 3.080 | 3.080 |
| Rmerge | 0.098 | 0.539 |
| Number of reflections | 12868 | |
| <I/σ(I)> | 31.5 | 4.2 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 7.7 | 7.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8 | 293 | 0.1M SPG buffer, 25% w/v PEG 1500, pH 8, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
