7B0K
membrane protein structure
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SLS BEAMLINE X06SA |
Synchrotron site | SLS |
Beamline | X06SA |
Temperature [K] | 298 |
Detector technology | PIXEL |
Collection date | 2018-02-02 |
Detector | DECTRIS EIGER X 16M |
Wavelength(s) | 1.0 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 128.900, 43.440, 126.820 |
Unit cell angles | 90.00, 120.43, 90.00 |
Refinement procedure
Resolution | 10.960 - 3.800 |
R-factor | 0.311 |
Rwork | 0.309 |
R-free | 0.32670 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | other |
RMSD bond length | 0.003 |
RMSD bond angle | 0.564 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | PHASER |
Refinement software | PHENIX (1.15.2_3472) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 12.995 | 15.790 | 3.950 |
High resolution limit [Å] | 3.530 | 11.160 | 3.830 |
Rmerge | 0.121 | 0.060 | 0.571 |
Rmeas | 0.146 | 0.072 | 0.677 |
Total number of observations | 18226 | ||
Number of reflections | 5593 | 149 | 196 |
<I/σ(I)> | 3.94 | 9.24 | 2.32 |
Completeness [%] | 72.1 | 89.2 | 37.2 |
Redundancy | 3.259 | 2.772 | 3.52 |
CC(1/2) | 0.996 | 0.995 | 0.851 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION | 289 | 30 % PEG 400, 50 mM HEPES pH 6.4 |