3HAP
Crystal structure of bacteriorhodopsin mutant L111A crystallized from bicelles
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ALS BEAMLINE 8.2.2 |
Synchrotron site | ALS |
Beamline | 8.2.2 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2009-01-17 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 0.9998 |
Spacegroup name | C 2 2 21 |
Unit cell lengths | 44.951, 102.135, 128.027 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 21.740 - 1.600 |
R-factor | 0.169 |
Rwork | 0.167 |
R-free | 0.19200 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.010 |
RMSD bond angle | 2.007 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.660 |
High resolution limit [Å] | 1.600 | 1.600 |
Rmerge | 0.050 | 0.382 |
Number of reflections | 36787 | |
<I/σ(I)> | 22.431 | |
Completeness [%] | 93.9 | 78.4 |
Redundancy | 6.3 | 4.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | hanging drop, bicelle method | 4 | 310 | 400ul 4M NaPi, 30ul 6M 1,6-hexanediol, 35ul 100% triethylene glycol, 535 ul H2O, pH 4.0, hanging drop, bicelle method, temperature 310K |