5KKH
2.1-Angstrom In situ Mylar structure of bacteriorhodopsin from Haloquadratum walsbyi (HwBR) at 100 K
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 23-ID-D |
Synchrotron site | APS |
Beamline | 23-ID-D |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2016-03-11 |
Detector | DECTRIS PILATUS 6M |
Wavelength(s) | 1.0 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 106.110, 61.270, 119.030 |
Unit cell angles | 90.00, 116.26, 90.00 |
Refinement procedure
Resolution | 29.446 - 2.125 |
R-factor | 0.2138 |
Rwork | 0.213 |
R-free | 0.23300 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2ei4 |
RMSD bond length | 0.009 |
RMSD bond angle | 1.774 |
Data reduction software | XDS |
Data scaling software | Aimless |
Phasing software | PHASER |
Refinement software | PHENIX ((1.10.1_2155)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 29.450 | 2.200 |
High resolution limit [Å] | 2.125 | 2.130 |
Rmerge | 0.107 | 0.250 |
Number of reflections | 35323 | |
<I/σ(I)> | 6.26 | 3.66 |
Completeness [%] | 91.0 | 70 |
Redundancy | 1.8 | 1.8 |
CC(1/2) | 0.960 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | LIPIDIC CUBIC PHASE | 7 | 293 | 8% (v/v) Tacsimate, 20% (v/v) PEG 3350 |