3JR3
Sir2 bound to acetylated peptide
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 14-BM-C |
| Synchrotron site | APS |
| Beamline | 14-BM-C |
| Detector technology | CCD |
| Collection date | 2007-03-17 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.95 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 45.717, 58.382, 106.516 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 22.550 - 1.500 |
| R-factor | 0.20578 |
| Rwork | 0.205 |
| R-free | 0.22787 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2h2d |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.203 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 22.550 |
| High resolution limit [Å] | 1.500 |
| Rmerge | 0.110 |
| Number of reflections | 43439 |
| <I/σ(I)> | 4.32 |
| Completeness [%] | 98.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 9.2 | 298 | pH 9.2, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
