8AH2
Crystal structure of human 14-3-3 zeta fused to the NPM1 peptide including phosphoserine-48
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2022-06-07 |
| Detector | RIGAKU HyPix-6000HE |
| Wavelength(s) | 1.54184 |
| Spacegroup name | I 21 21 21 |
| Unit cell lengths | 79.696, 110.207, 163.413 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 21.910 - 2.900 |
| R-factor | 0.2722 |
| Rwork | 0.270 |
| R-free | 0.32260 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 6fnc |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.363 |
| Data reduction software | CrysalisPro |
| Data scaling software | Aimless (0.7.8) |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.8.0352) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 21.910 | 21.910 | 3.080 |
| High resolution limit [Å] | 2.900 | 8.700 | 2.900 |
| Rmerge | 0.157 | 0.022 | 1.659 |
| Rmeas | 0.168 | 0.025 | 1.761 |
| Rpim | 0.058 | 0.011 | 0.584 |
| Total number of observations | 131674 | 3012 | 23356 |
| Number of reflections | 16235 | 618 | 2602 |
| <I/σ(I)> | 10.4 | 40.4 | 1 |
| Completeness [%] | 99.5 | 92.7 | 100 |
| Redundancy | 8.1 | 4.9 | 9 |
| CC(1/2) | 0.999 | 0.999 | 0.883 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 288 | 0.01 M CoCl2, 0.1 M MES, pH 6.5, 2.2 M (NH4)2SO4 |
