2VKJ
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 21 21 2 |
| Unit cell lengths | 68.229, 76.199, 46.230 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 50.830 - 1.650 |
| R-factor | 0.205 |
| Rwork | 0.203 |
| R-free | 0.22900 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.379 |
| 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 | 1.700 |
| High resolution limit [Å] | 1.650 | 1.650 |
| Rmerge | 0.060 | 0.350 |
| Number of reflections | 27259 | |
| <I/σ(I)> | 29 | 2.9 |
| Completeness [%] | 96.6 | 88 |
| Redundancy | 3.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 6.5 | 30% PEG400, 0.2 M LI2SO4, 0.1 M NACACODYLATE, PH 6.5 |
