3P1N
Crystal structure of human 14-3-3 sigma in complex with TASK-3 peptide
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SLS BEAMLINE X10SA |
| Synchrotron site | SLS |
| Beamline | X10SA |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2009-02-16 |
| Detector | MARMOSAIC 225 mm CCD |
| Wavelength(s) | 0.84999 |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 82.220, 112.050, 62.510 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 45.500 - 1.400 |
| R-factor | 0.14949 |
| Rwork | 0.148 |
| R-free | 0.17449 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3lw1 |
| RMSD bond length | 0.029 |
| RMSD bond angle | 2.553 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 45.500 | 1.450 |
| High resolution limit [Å] | 1.400 | 1.400 |
| Rmerge | 0.077 | 0.347 |
| Number of reflections | 57021 | |
| <I/σ(I)> | 15.89 | 5.22 |
| Completeness [%] | 99.8 | 99.8 |
| Redundancy | 6.59 | 4.59 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.4 | 277 | 0.095M HEPES Na-Salt, 25.6% PEG 400, 0.19M CaCl2, 5% Glycerol, pH 7.4, VAPOR DIFFUSION, HANGING DROP, temperature 277K |
