5AXK
Crystal structure of Thg1 like protein (TLP)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SPRING-8 BEAMLINE BL41XU |
| Synchrotron site | SPring-8 |
| Beamline | BL41XU |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2013-06-20 |
| Detector | RAYONIX MX225HE |
| Wavelength(s) | 0.978 |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 98.255, 120.480, 157.392 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 46.896 - 2.290 |
| R-factor | 0.2084 |
| Rwork | 0.206 |
| R-free | 0.23950 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3wbz |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.109 |
| Data reduction software | XDS |
| Data scaling software | XDS |
| Phasing software | PHASER |
| Refinement software | PHENIX ((phenix.refine: 1.9_1692)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.430 |
| High resolution limit [Å] | 2.290 | 2.290 |
| Rmerge | 0.700 | |
| Number of reflections | 41650 | |
| <I/σ(I)> | 14.7 | 2.8 |
| Completeness [%] | 98.3 | 93.8 |
| Redundancy | 6.7 | 6.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 293 | PEG 3350, tri-potassium citrate |
