3PDH
Structure of Sir2Tm bound to a propionylated peptide
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 14-BM-C |
| Synchrotron site | APS |
| Beamline | 14-BM-C |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2008-04-14 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.9002 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 46.561, 60.013, 106.345 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 30.010 - 1.800 |
| R-factor | 0.16715 |
| Rwork | 0.165 |
| R-free | 0.21010 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2h4f |
| RMSD bond length | 0.020 |
| RMSD bond angle | 1.612 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.010 | 1.850 |
| High resolution limit [Å] | 1.800 | 1.800 |
| Rmerge | 0.099 | 0.639 |
| Number of reflections | 28346 | |
| <I/σ(I)> | 23.8 | 2.9 |
| Completeness [%] | 99.8 | 99.3 |
| Redundancy | 7 | 6.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 293 | Crystals were obtained from 1:1 mix of protein and the well solution (9.5% (w/v) PEG3350, 100 mM CHES buffer), pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
