1GJU
Maltosyltransferase from Thermotoga maritima
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SRS BEAMLINE PX7.2 |
| Synchrotron site | SRS |
| Beamline | PX7.2 |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Detector | MARRESEARCH |
| Spacegroup name | P 41 2 2 |
| Unit cell lengths | 148.740, 148.740, 106.700 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 10.000 - 2.400 |
| R-factor | 0.208 |
| Rwork | 0.208 |
| R-free | 0.26300 |
| Structure solution method | MIR |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.500 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | CCP4 |
| Refinement software | CNS (0.9) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 2.420 |
| High resolution limit [Å] | 2.400 | 2.380 |
| Rmerge | 0.047 | 0.138 |
| Total number of observations | 198549 * | |
| Number of reflections | 47952 | |
| <I/σ(I)> | 23.9 | 9.9 |
| Completeness [%] | 99.0 | 98 |
| Redundancy | 4.2 | 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) |
