3HAQ
Crystal structure of bacteriorhodopsin mutant I148A 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 | 2008-04-14 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 1.00000 |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 44.998, 102.211, 127.970 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 39.940 - 2.300 |
| R-factor | 0.182 |
| Rwork | 0.178 |
| R-free | 0.23600 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.020 |
| RMSD bond angle | 2.233 |
| 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 | 2.380 |
| High resolution limit [Å] | 2.300 | 2.300 |
| Rmerge | 0.103 | 0.442 |
| Number of reflections | 12778 | |
| <I/σ(I)> | 9.048 | |
| Completeness [%] | 94.3 | 92.6 |
| Redundancy | 3.7 | 2.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | hanging drop, bicelle method | 3.9 | 310 | 2.2 M sodium phosphate, 180 mM 1,6-hexanediol, 3.5 % triethylene glycol, PFPC used as cryoprotectant, pH 3.9, hanging drop, bicelle method, temperature 310K |
