1GJW
Thermotoga maritima maltosyltransferase complex with maltose
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SRS BEAMLINE PX9.6 |
Synchrotron site | SRS |
Beamline | PX9.6 |
Temperature [K] | 100 |
Detector technology | CCD |
Spacegroup name | P 41 2 2 |
Unit cell lengths | 147.390, 147.390, 105.630 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 10.000 - 2.100 |
R-factor | 0.197 |
Rwork | 0.197 |
R-free | 0.25200 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | FREE ENZYME |
RMSD bond length | 0.012 |
RMSD bond angle | 1.500 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | CNS |
Refinement software | CNS (0.9) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 2.170 |
High resolution limit [Å] | 2.100 | 2.130 |
Rmerge | 0.044 | 0.247 |
Total number of observations | 105717 * | |
Number of reflections | 53029 | |
<I/σ(I)> | 17.9 | 3.7 |
Completeness [%] | 81.0 * | 56 * |
Redundancy | 2 | 1.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 4.8 | 290 * | Burke, J., (2000) Acta Crystallog., D56, 1049. * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | Tris-HCl | 50 (mM) | |
2 | 1 | drop | 150 (mM) | ||
3 | 1 | drop | protein | 18 (mg/ml) | |
4 | 1 | reservoir | ammonium phosphate | 0.35-0.40 (M) |