1LR5
Crystal structure of auxin binding protein
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SRS BEAMLINE PX9.6 |
| Synchrotron site | SRS |
| Beamline | PX9.6 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Detector | ADSC QUANTUM 4 |
| Wavelength(s) | 0.87 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 61.583, 82.433, 69.962 |
| Unit cell angles | 90.00, 94.37, 90.00 |
Refinement procedure
| Resolution | 15.000 - 1.900 |
| R-factor | 0.19 |
| Rwork | 0.184 |
| R-free | 0.24100 |
| Structure solution method | MIR |
| RMSD bond length | 0.014 * |
| RMSD bond angle | 0.033 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | MLPHARE |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 1.970 |
| High resolution limit [Å] | 1.900 | 1.900 |
| Rmerge | 0.040 | 0.116 |
| Number of reflections | 53947 | |
| Completeness [%] | 99.0 | 91.1 * |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 7 * | 291 * | Woo, E.J., (2000) Acta Crystallogr., Sect.D, 56, 1476. * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | reservoir | Tris | 20 (mM) | pH7.0 |
| 2 | 1 | reservoir | 1 (mM) | ||
| 3 | 1 | reservoir | sodium azide | 2 (mM) | |
| 4 | 1 | drop | protein | 8.5 (mg/ml) |
