2H4H
Sir2 H116Y mutant-p53 peptide-NAD
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 14-BM-D |
| Synchrotron site | APS |
| Beamline | 14-BM-D |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2005-02-07 |
| Detector | ADSC QUANTUM 4 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 42.260, 58.676, 106.846 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 50.000 - 1.990 |
| R-factor | 0.1977 |
| Rwork | 0.196 |
| R-free | 0.23683 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | : 1yc5 |
| RMSD bond length | 0.019 |
| RMSD bond angle | 1.947 |
| 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 | 20058 |
| Completeness [%] | 99.4 |
| Redundancy | 6.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 9.6 | 293 | CHES, PEG 3350, pH9.6, NAD, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
