3HAS
Crystal structure of bacteriorhodopsin mutant L152A crystallized from bicelles
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ALS BEAMLINE 8.2.1 |
| Synchrotron site | ALS |
| Beamline | 8.2.1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2008-04-13 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 1.00000 |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 45.169, 102.348, 128.271 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 27.230 - 1.900 |
| R-factor | 0.174 |
| Rwork | 0.171 |
| R-free | 0.20200 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.014 |
| RMSD bond angle | 1.905 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 90.000 | 1.970 |
| High resolution limit [Å] | 1.900 | 1.900 |
| Rmerge | 0.126 | 0.413 |
| Number of reflections | 23760 | |
| <I/σ(I)> | 13.945 | |
| Completeness [%] | 99.2 | 93 |
| Redundancy | 7.4 | 2.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | hanging drop, bicelle method | 4 | 310 | 1.68 M sodium phosphate, 180 mM 1,6-hexanediol, 3.5 % triethylene glycol, PFPC used as cryoprotectant, pH 4.0, hanging drop, bicelle method, temperature 310K |
