8A8Q
Crystal structure of Protein Scalloped in complex with YAP 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 | PIXEL |
| Collection date | 2019-11-19 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 1.0000 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 42.772, 85.700, 76.227 |
| Unit cell angles | 90.00, 92.62, 90.00 |
Refinement procedure
| Resolution | 29.090 - 1.465 |
| R-factor | 0.2119 |
| Rwork | 0.211 |
| R-free | 0.23370 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | Previous in-house structure. |
| RMSD bond length | 0.008 |
| RMSD bond angle | 0.990 |
| Data reduction software | autoPROC |
| Data scaling software | STARANISO |
| Phasing software | PHASER |
| Refinement software | BUSTER (2.11.8 (3-FEB-2022)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 76.147 | 1.673 |
| High resolution limit [Å] | 1.472 | 1.472 |
| Rmerge | 0.084 | 0.691 |
| Rmeas | 0.094 | 0.800 |
| Rpim | 0.041 | 0.397 |
| Number of reflections | 52439 | 2623 |
| <I/σ(I)> | 10.1 | 1.8 |
| Completeness [%] | 56.5 | 8.9 |
| Redundancy | 5 | 3.5 |
| CC(1/2) | 0.998 | 0.630 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 293 | 0.1 M MES pH 6 20 % PEG8000 0.2 M sodium acetate trihydrate |
