1PYB
Crystal Structure of Aquifex aeolicus Trbp111: a Structure-Specific tRNA Binding Protein
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SSRL BEAMLINE BL7-1 |
Synchrotron site | SSRL |
Beamline | BL7-1 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 1999-08-03 |
Detector | MARRESEARCH |
Wavelength(s) | 1.08 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 145.400, 72.790, 68.940 |
Unit cell angles | 90.00, 91.93, 90.00 |
Refinement procedure
Resolution | 20.000 - 2.500 |
R-factor | 0.226 |
Rwork | 0.208 |
R-free | 0.22000 * |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1PXF |
RMSD bond length | 0.005 |
RMSD bond angle | 1.600 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | CNS |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.440 |
High resolution limit [Å] | 2.400 | 2.400 |
Rmerge | 0.042 * | 0.361 * |
Number of reflections | 26611 | |
<I/σ(I)> | 9.7 | 2.9 |
Completeness [%] | 94.0 | 88.4 |
Redundancy | 2.1 | 1.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.2 | 17 * | PEG2000, ammonium sulfate, imidazole, pH 7.2, VAPOR DIFFUSION, HANGING DROP, temperature 290.15K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | PEG2000 | 30 (%) | |
2 | 1 | drop | ammonium sulfate | 0.24 (M) | |
3 | 1 | drop | imidazole | 0.1 (M) | pH7.2 |
4 | 1 | drop | protein | 24 (mg/ml) |