1KN0
Crystal Structure of the human Rad52 protein
Experimental procedure
| Experimental method | MAD |
| Source type | SYNCHROTRON |
| Source details | SPRING-8 BEAMLINE BL45PX |
| Synchrotron site | SPring-8 |
| Beamline | BL45PX |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2001-04-27 |
| Detector | RIGAKU RAXIS |
| Wavelength(s) | 0.979, 0.9795, 1.02 |
| Spacegroup name | P 43 21 2 |
| Unit cell lengths | 145.610, 145.610, 247.530 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 50.000 - 2.850 |
| R-factor | 0.2361 |
| Rwork | 0.231 |
| R-free | 0.29700 |
| Structure solution method | MAD |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.250 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | SHARP |
| Refinement software | CNS |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.900 |
| High resolution limit [Å] | 2.850 | 2.850 |
| Rmerge | 0.073 * | 0.404 * |
| Total number of observations | 1378830 * | |
| Number of reflections | 63100 * | |
| Completeness [%] | 99.7 | 99.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.2 | 20 * | PEG 5000MME, ammonium sulfate, sodium cacodylate, pH 6.2, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 3-3.5 (mg/ml) | |
| 2 | 1 | drop | PEG5000 MME | 12 (%) | |
| 3 | 1 | drop | ammonium sulfate | 80 (mM) | |
| 4 | 1 | drop | betaine monohydrate | 20 (mM) | or urea |
| 5 | 1 | drop | sodium cacodylate | 40 (mM) | pH6.2 |
| 6 | 1 | reservoir | PEG5000 MME | 15 (%) | |
| 7 | 1 | reservoir | ammonium sulfate | 0.1 (M) | |
| 8 | 1 | reservoir | sodium cacodylate | 50 (mM) | pH6.2 |
