2H4F
Sir2-p53 peptide-NAD+
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 24-ID-C |
| Synchrotron site | APS |
| Beamline | 24-ID-C |
| Temperature [K] | 77.36 |
| Detector technology | CCD |
| Collection date | 2005-07-03 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 1.0 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 45.821, 59.331, 106.660 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 50.000 - 2.000 |
| R-factor | 0.19406 |
| Rwork | 0.192 |
| R-free | 0.22823 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | : 1yc5 |
| RMSD bond length | 0.017 |
| RMSD bond angle | 1.780 |
| Data scaling software | HKL-2000 |
| Phasing software | CNS |
| Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 50.000 |
| High resolution limit [Å] | 2.000 |
| Number of reflections | 20048 |
| Completeness [%] | 98.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 9.6 | 293 | CHES, PEG3350, NAD, pH 9.6, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
