1II8
Crystal structure of the P. furiosus Rad50 ATPase domain
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ALS BEAMLINE 5.0.2 |
| Synchrotron site | ALS |
| Beamline | 5.0.2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2000-08-26 |
| Detector | ADSC QUANTUM 4 |
| Wavelength(s) | 0.9 |
| Spacegroup name | P 31 2 1 |
| Unit cell lengths | 99.531, 99.531, 116.407 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 28.840 - 3.020 |
| R-factor | 0.255 |
| Rwork | 0.255 |
| R-free | 0.29400 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1f2t |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.600 |
| Data reduction software | DENZO |
| Data scaling software | CCP4 ((TRUNCATE)) |
| Phasing software | AMoRE |
| Refinement software | CNS (1.0) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 3.110 |
| High resolution limit [Å] | 3.000 | 3.000 |
| Rmerge | 0.057 | 0.348 |
| Total number of observations | 119376 * | |
| Number of reflections | 13527 * | |
| <I/σ(I)> | 7.1 | |
| Completeness [%] | 83.0 | 47.3 |
| Redundancy | 8.8 | 2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.5 * | 300 | 100 mM Na-Acetate, 8% PEG 6K, 10 mM Ca-Acetate, pH 6.2, VAPOR DIFFUSION, SITTING DROP, temperature 300K |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 8 (mg/ml) | |
| 2 | 1 | drop | phosphate | 20 (mM) | |
| 3 | 1 | drop | 200 (mM) | ||
| 4 | 1 | drop | EDTA | 0.1 (mM) | |
| 5 | 1 | drop | glycerol | 5 (%) | |
| 6 | 1 | reservoir | sodium acetate | 100 (mM) | |
| 7 | 1 | reservoir | PEG6000 | 8 (%) | |
| 8 | 1 | reservoir | calcium acetate | 10 (mM) |
