3FRQ
Structure of the macrolide biosensor protein, MphR(A), with erythromcyin
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 24-ID-C |
| Synchrotron site | APS |
| Beamline | 24-ID-C |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2008-05-22 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.9795 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 44.294, 61.201, 134.642 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 67.270 - 1.760 |
| R-factor | 0.18303 |
| Rwork | 0.181 |
| R-free | 0.22130 |
| Structure solution method | SAD |
| RMSD bond length | 0.016 |
| RMSD bond angle | 1.554 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | SHELXS |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 67.270 | |
| High resolution limit [Å] | 1.760 | 1.760 |
| Number of reflections | 35192 | |
| Completeness [%] | 100.0 | 100 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5.5 | 293 | 35-40% (W/V) PEG 3350, 0.2M MgCl2, 0.1M Bis-Tris, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
