1L1O
Structure of the human Replication Protein A (RPA) trimerization core
Experimental procedure
| Experimental method | MAD |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 19-ID |
| Synchrotron site | APS |
| Beamline | 19-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 1999-09-05 |
| Detector | ADSC QUANTUM 4 |
| Wavelength(s) | 1.008 |
| Spacegroup name | P 31 2 1 |
| Unit cell lengths | 88.527, 88.527, 341.090 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 19.920 - 2.800 |
| R-factor | 0.236 |
| Rwork | 0.236 |
| R-free | 0.28300 * |
| Structure solution method | MAD |
| RMSD bond length | 0.019 * |
| RMSD bond angle | 25.500 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | SHARP |
| Refinement software | CNS (1.0) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 2.800 |
| High resolution limit [Å] | 2.700 | 2.700 |
| Rmerge | 0.062 * | 0.532 * |
| Total number of observations | 233991 * | |
| Number of reflections | 43573 | |
| <I/σ(I)> | 2.7 | 2.7 |
| Completeness [%] | 99.2 | 99.7 |
| Redundancy | 5.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.8 | 300 | Bochkareva, E., (2000) J.Biol.Chem., 275, 27332. * |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.8 | 300 | Bochkareva, E., (2000) J.Biol.Chem., 275, 27332. * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | reservoir | HEPES | 0.1 (M) | pH7.8 |
| 2 | 1 | reservoir | glycerol | 9 (%) | |
| 3 | 1 | reservoir | ammonium sulfate | 1.6 (M) |
