1GXK
SMC hinge domain from T. maritima w/o coiled coil, P212121 crystal form
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE BM14 |
Synchrotron site | ESRF |
Beamline | BM14 |
Temperature [K] | 100 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 58.900, 62.210, 225.120 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 30.000 - 3.000 |
R-factor | 0.253 * |
Rwork | 0.253 |
R-free | 0.29800 * |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | P21 CRYSTAL FORM PDB ID 1GXJ |
RMSD bond length | 0.009 |
RMSD bond angle | 1.332 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | CNS |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 3.160 |
High resolution limit [Å] | 3.000 | 3.000 |
Rmerge | 0.093 | 0.235 |
Number of reflections | 13536 | |
<I/σ(I)> | 10.6 | 3.1 |
Completeness [%] | 92.7 | 92.6 |
Redundancy | 2.8 | 2.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, sitting drop * | 6.9 * | 19 * | pH 9.20 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | reservoir | PEG2000 MME | 15 (%) | |
2 | 1 | reservoir | Tris | 0.1 (M) | pH6.9 |
3 | 1 | drop | protein | 10 (mg/ml) |