1GXJ
SMC hinge domain from T. maritima w/o coiled coil
Experimental procedure
Experimental method | MAD |
Source type | SYNCHROTRON |
Source details | SRS BEAMLINE PX9.5 |
Synchrotron site | SRS |
Beamline | PX9.5 |
Temperature [K] | 100 |
Wavelength(s) | 0.9793, 0.9798, 0.93 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 54.700, 57.900, 62.500 |
Unit cell angles | 90.00, 113.40, 90.00 |
Refinement procedure
Resolution | 20.000 - 2.000 |
R-factor | 0.226 * |
Rwork | 0.226 |
R-free | 0.26700 * |
Structure solution method | MAD |
RMSD bond length | 0.005 |
RMSD bond angle | 1.135 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | SOLVE |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 2.110 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.072 | 0.185 |
Number of reflections | 16848 | |
<I/σ(I)> | 12.2 | 4.3 |
Completeness [%] | 95.0 | 93.7 |
Redundancy | 2.2 | 2.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, sitting drop * | 9.2 | 19 * | pH 9.20 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | reservoir | PEG3000 | 26 (%) | |
2 | 1 | reservoir | CHES | 0.1 (M) | pH9.2 |
3 | 1 | drop | protein | 20 (mg/ml) |