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 |