6BQT
Complex of 14-3-3 theta with an IRSp53 peptide doubly-phosphorylated at T340 and T360
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SEALED TUBE |
| Source details | BRUKER IMUS MICROFOCUS |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2015-07-29 |
| Detector | APEX II CCD |
| Wavelength(s) | 1.540 |
| Spacegroup name | P 1 |
| Unit cell lengths | 61.103, 69.572, 150.473 |
| Unit cell angles | 99.16, 92.98, 115.98 |
Refinement procedure
| Resolution | 42.983 - 2.800 |
| R-factor | 0.236 |
| Rwork | 0.234 |
| R-free | 0.28670 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2br9 |
| RMSD bond length | 0.003 |
| RMSD bond angle | 0.548 |
| Data reduction software | PROTEUM2 |
| Data scaling software | SAINT |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.12_2829) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 49.000 | 2.900 |
| High resolution limit [Å] | 2.800 | 2.800 |
| Rmerge | 0.142 | 0.293 |
| Number of reflections | 51911 | 5197 |
| <I/σ(I)> | 20.5 | 2.5 |
| Completeness [%] | 96.7 | 95.7 |
| Redundancy | 4.8 | 2.1 |
| CC(1/2) | 0.975 | 0.717 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7 | 291.15 | 0.1 M CaCl2, 13% Peg 3350 |
