5AXM
Crystal structure of Thg1 like protein (TLP) with tRNA(Phe)
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | PHOTON FACTORY BEAMLINE BL-17A |
Synchrotron site | Photon Factory |
Beamline | BL-17A |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2013-11-30 |
Detector | ADSC QUANTUM 270 |
Wavelength(s) | 0.97319 |
Spacegroup name | I 2 2 2 |
Unit cell lengths | 75.258, 127.582, 143.801 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 48.144 - 2.210 |
R-factor | 0.2169 |
Rwork | 0.215 |
R-free | 0.24270 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3wbz 1ehz |
RMSD bond length | 0.007 |
RMSD bond angle | 0.717 |
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 | 2.340 |
High resolution limit [Å] | 2.210 | 2.210 |
Rmerge | 0.692 | |
Number of reflections | 35102 | |
<I/σ(I)> | 19.4 | 3.2 |
Completeness [%] | 99.7 | 98.6 |
Redundancy | 7.4 | 7.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 8 | 293 | PEG 3350, tri-potassium citrate |