9G76
Crystal structure of ASGPR with bound GalNAc
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SLS BEAMLINE X06SA |
Synchrotron site | SLS |
Beamline | X06SA |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2017-12-13 |
Detector | DECTRIS EIGER X 16M |
Wavelength(s) | 0.999910 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 114.082, 32.641, 40.702 |
Unit cell angles | 90.00, 91.89, 90.00 |
Refinement procedure
Resolution | 40.680 - 1.199 |
R-factor | 0.2004 |
Rwork | 0.199 |
R-free | 0.23340 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.008 |
RMSD bond angle | 0.880 |
Data reduction software | autoPROC |
Data scaling software | autoPROC (1.1.7) |
Phasing software | BUSTER |
Refinement software | BUSTER (2.11.8 (20-OCT-2021)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 40.680 | 1.357 |
High resolution limit [Å] | 1.199 | 1.199 |
Rmerge | 0.087 | 1.164 |
Number of reflections | 27219 | 1361 |
<I/σ(I)> | 9.6 | 1.6 |
Completeness [%] | 57.6 | 9.3 |
Redundancy | 3.2 | 3.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 293 | PROTEIN BUFFER: 20 MM TRIS-HCL (PH 7.4), 25 MM CACL2. RESERVOIR: 100 MM TRIS-HCL (PH 7.5), 28% PEG4000, PH 7.50, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K |