3H0X
Crystal structure of peptide-binding domain of Kar2 protein from Saccharomyces cerevisiae
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 19-ID |
| Synchrotron site | APS |
| Beamline | 19-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2008-06-15 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.9792 |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 41.846, 103.113, 80.792 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 35.100 - 1.920 |
| R-factor | 0.188 |
| Rwork | 0.186 |
| R-free | 0.23000 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2op6 |
| RMSD bond length | 0.018 |
| RMSD bond angle | 1.581 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | HKL-3000 |
| Refinement software | REFMAC (5.5.0054) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 35.100 | 1.950 |
| High resolution limit [Å] | 1.920 | 1.920 |
| Rmerge | 0.067 | 0.806 |
| Number of reflections | 13673 | |
| <I/σ(I)> | 31.919 | 2 |
| Completeness [%] | 99.7 | 98.5 |
| Redundancy | 7 | 5.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 5.6 | 277 | 0.17 M Ammonium acetate, 0.085 M Sodium citrate, 25.5% PEG 4000, 15% Glycerol, pH 5.6, VAPOR DIFFUSION, SITTING DROP, temperature 277K |
