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 |