1PXR
Structure of Pro50Ala mutant of Bacteriorhodopsin
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ALS BEAMLINE 5.0.1 |
| Synchrotron site | ALS |
| Beamline | 5.0.1 |
| Temperature [K] | 110 |
| Detector technology | CCD |
| Collection date | 2002-08-11 |
| Detector | ADSC QUANTUM 4 |
| Wavelength(s) | 1.0 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 44.967, 108.839, 55.981 |
| Unit cell angles | 90.00, 113.60, 90.00 |
Refinement procedure
| Resolution | 26.420 - 1.700 |
| R-factor | 0.2072 |
| Rwork | 0.207 |
| R-free | 0.24600 * |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1c3w |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.100 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | CNS |
| Refinement software | CNS (1.1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.710 |
| High resolution limit [Å] | 1.700 * | 1.650 |
| Rmerge | 0.105 * | 0.223 * |
| Number of reflections | 50535 | |
| Completeness [%] | 85.4 | 53.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 3.5 | 37 * | Faham, S., (2002) J. Mol. Biol., 316, 1. * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | bR | 8.0 (mg/ml) | |
| 2 | 1 | drop | bicell | 8 (%) | |
| 3 | 1 | drop | beta-octylglucoside | 2.5 (%) | |
| 4 | 1 | reservoir | sodium phosphate | 3.2 (M) | pH3.5 |
