Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF |
| Synchrotron site | ESRF |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 68.597, 225.045, 70.349 |
| Unit cell angles | 90.00, 108.39, 90.00 |
Refinement procedure
| Resolution | 30.000 - 2.300 |
| Rwork | 0.188 |
| R-free | 0.22100 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1GTX |
| RMSD bond length | 0.009 * |
| RMSD bond angle | 1.100 * |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | CCP4 |
| Refinement software | REFMAC (5.1.24) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 * | 2.420 |
| High resolution limit [Å] | 2.300 * | 2.300 |
| Rmerge | 0.085 | 0.200 |
| Number of reflections | 80297 * | |
| <I/σ(I)> | 5.1 | 3.25 |
| Completeness [%] | 90.0 * | 93 |
| Redundancy | 2.0 * | 2.04 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, sitting drop * | 5.4 * | pH 5.70 |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 10-14 (mg/ml) | |
| 2 | 1 | drop | sodium acetate | 40 (mM) | pH5.4 |
| 3 | 1 | reservoir | PEG4000 | 16-18 (%) | |
| 4 | 1 | reservoir | glycerol | 0-10 (%) | |
| 5 | 1 | reservoir | sodium cacodylate | 50 (mM) | pH6.0 |
| 6 | 1 | reservoir | dithiothreitol | 1 (mM) |
