9D34
FIP200 C-terminal CLAW domain (resid. 1490-1594) in complex with phosphorylated TNIP1 FIP200 interacting peptide
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SSRL BEAMLINE BL12-1 |
| Synchrotron site | SSRL |
| Beamline | BL12-1 |
| Temperature [K] | 80 |
| Detector technology | PIXEL |
| Collection date | 2024-05-29 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 0.979460 |
| Spacegroup name | P 43 21 2 |
| Unit cell lengths | 51.339, 51.339, 88.280 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 33.570 - 1.420 |
| R-factor | 0.2037 |
| Rwork | 0.202 |
| R-free | 0.23400 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.254 |
| Data reduction software | XDS |
| Data scaling software | Aimless |
| Phasing software | PHASER |
| Refinement software | PHENIX ((1.20.1_4487: ???)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 33.570 | 1.471 |
| High resolution limit [Å] | 1.420 | 1.420 |
| Rmerge | 1.496 | |
| Rpim | 0.325 | |
| Number of reflections | 22984 | 1889 |
| <I/σ(I)> | 21.41 | |
| Completeness [%] | 96.3 | 83.99 |
| Redundancy | 20 | |
| CC(1/2) | 0.996 | 0.814 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 293 | Morpheus E4 (12.5% w/v PEG 1000, 12.5% w/v PEG 3350, 12.5% v/v MPD, 0.03 M of each ethylene glycol, 0.1 M MES/imidazole pH 6.5) |






