4HB7
The Structure of Dihydropteroate Synthase from Staphylococcus aureus subsp. aureus Mu50.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 19-ID |
| Synchrotron site | APS |
| Beamline | 19-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2011-12-11 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.97907 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 90.584, 77.301, 90.546 |
| Unit cell angles | 90.00, 99.75, 90.00 |
Refinement procedure
| Resolution | 27.800 - 1.950 |
| R-factor | 0.1645 |
| Rwork | 0.162 |
| R-free | 0.20560 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1ad1 |
| RMSD bond length | 0.015 |
| RMSD bond angle | 1.615 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | HKL-3000 |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 1.920 |
| High resolution limit [Å] | 1.900 | 5.900 | 1.900 |
| Rmerge | 0.053 | 0.026 | 0.200 |
| Number of reflections | 42672 | ||
| <I/σ(I)> | 10 | ||
| Completeness [%] | 88.3 | 95.2 | 62.9 |
| Redundancy | 3.7 | 3.6 | 2.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 289 | 0.2M MgCl2, 0.1MES:NaOH pH 6.5, 10% PEG 4K, VAPOR DIFFUSION, HANGING DROP, temperature 289K |
