2VKO
Structure of the soluble domain of the membrane protein TM1634 from Thermotoga maritima
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ALS BEAMLINE 5.0.1 |
| Synchrotron site | ALS |
| Beamline | 5.0.1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2006-04-07 |
| Detector | ADSC CCD |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 50.852, 81.973, 68.327 |
| Unit cell angles | 90.00, 101.41, 90.00 |
Refinement procedure
| Resolution | 66.960 - 1.790 |
| R-factor | 0.243 |
| Rwork | 0.241 |
| R-free | 0.27700 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2vkj |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.310 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.840 |
| High resolution limit [Å] | 1.800 | 1.800 |
| Rmerge | 0.080 | 0.570 |
| Number of reflections | 51063 | |
| <I/σ(I)> | 17.9 | |
| Completeness [%] | 99.2 | 99.6 |
| Redundancy | 3.2 | 3.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 5.5 | 50% PEG200, 0.1 M NACITRATE PH 5.5 |
