6Y20
Crystal structure of Protein Scalloped (222-440) bound to Protein Vestigial (298-337)
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 | 2019-11-29 |
Detector | DECTRIS EIGER X 16M |
Wavelength(s) | 1.0 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 48.230, 62.039, 156.887 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 78.000 - 1.849 |
R-factor | 0.1894 |
Rwork | 0.188 |
R-free | 0.22160 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 6q36 |
RMSD bond length | 0.008 |
RMSD bond angle | 0.990 |
Data reduction software | autoPROC |
Data scaling software | STARANISO |
Phasing software | PHASER |
Refinement software | BUSTER (2.11.7 (3-OCT-2019)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 78.444 | 2.013 |
High resolution limit [Å] | 1.851 | 1.851 |
Number of reflections | 30608 | 1531 |
<I/σ(I)> | 9.337 | 1.6 |
Completeness [%] | 74.6 | 16.9 |
Redundancy | 16.7 | |
CC(1/2) | 0.994 | 0.619 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 293 | 0.2 M Magnesium chloride, 0.1 M Bis-Tris pH 6.5, 25% PEG3350 |