4NPF
High-resolution structure of two tandem B domains of staphylococcal protein A connected by the conserved linker
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 22-ID |
| Synchrotron site | APS |
| Beamline | 22-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2013-07-29 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 1.0 |
| Spacegroup name | P 65 |
| Unit cell lengths | 44.412, 44.412, 214.790 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 37.860 - 1.490 |
| R-factor | 0.1446 |
| Rwork | 0.142 |
| R-free | 0.18470 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.003 |
| RMSD bond angle | 0.692 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | PHENIX (1.8.3_1479) |
| Refinement software | PHENIX (1.8.3_1479) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 1.520 |
| High resolution limit [Å] | 1.490 | 4.040 | 1.490 |
| Rmerge | 0.101 | 0.059 | 0.616 |
| Number of reflections | 39130 | ||
| <I/σ(I)> | 7.5 | ||
| Completeness [%] | 99.9 | 99.3 | 99.6 |
| Redundancy | 6.8 | 5.3 | 4.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6 | 298 | Ammonium Sulfate, MES, pH 6, vapor diffusion, sitting drop, temperature 298K |
