1MA3
Structure of a Sir2 enzyme bound to an acetylated p53 peptide
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSLS BEAMLINE X25 |
| Synchrotron site | NSLS |
| Beamline | X25 |
| Temperature [K] | 93 |
| Detector technology | CCD |
| Collection date | 2001-07-20 |
| Detector | BRANDEIS - B4 |
| Wavelength(s) | 1.1 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 34.892, 35.591, 184.683 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 50.000 - 2.000 |
| R-factor | 0.211 |
| Rwork | 0.209 |
| R-free | 0.25400 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1ici |
| RMSD bond length | 0.006 |
| RMSD bond angle | 23.440 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP |
| Refinement software | CNS (1.0) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | |
| High resolution limit [Å] | 2.000 | 2.000 |
| Rmerge | 0.113 * | 0.342 * |
| Total number of observations | 79201 * | |
| Number of reflections | 15490 | 1414 * |
| <I/σ(I)> | 11.8 | 4.2 |
| Completeness [%] | 97.6 | 92.4 |
| Redundancy | 5.1 | 3.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5.5 | 20 * | PEG 8000, PEG 1000 and Sodium Chloride, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | Sir2-Af2 | 10 (mg/ml) | |
| 2 | 1 | drop | JB12 | 1.5 (mM) | |
| 3 | 1 | reservoir | MES | 40 (mM) | pH5.5 |
| 4 | 1 | reservoir | PEG8000 | 10 (%) | |
| 5 | 1 | reservoir | PEG1000 | 14 (%) | |
| 6 | 1 | reservoir | 5 (mM) |
