3SPR
Crystal structure of human 14-3-3 sigma C38V/N166H in complex with TASK-3 peptide and stabilizer FC-THF
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | BRUKER AXS MICROSTAR |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2010-08-04 |
| Detector | MAR scanner 345 mm plate |
| Wavelength(s) | 1.5418 |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 79.900, 109.200, 61.310 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 19.770 - 1.990 |
| R-factor | 0.1925 |
| Rwork | 0.190 |
| R-free | 0.25010 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3lw1 |
| RMSD bond length | 0.021 |
| RMSD bond angle | 2.038 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.5.0102) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 19.800 | 19.773 | 2.000 |
| High resolution limit [Å] | 1.990 | 10.000 | 1.990 |
| Rmerge | 0.057 | 0.021 | 0.585 |
| Number of reflections | 18617 | 144 | 259 |
| <I/σ(I)> | 25.53 | 48.38 | 4.07 |
| Completeness [%] | 99.2 | 81.4 | 99.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.4 | 277 | 0.095M HEPES Na-Salt pH7.4, 25.6% PEG 400, 0.19M CaCl2, 5% Glycerol, VAPOR DIFFUSION, HANGING DROP, temperature 277K |
