1D2R
2.9 A CRYSTAL STRUCTURE OF LIGAND-FREE TRYPTOPHANYL-TRNA SYNTHETASE: DOMAIN MOVEMENTS FRAGMENT THE ADENINE NUCLEOTIDE BINDING SITE.
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU200 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 226.760, 91.660, 156.970 |
Unit cell angles | 90.00, 132.66, 90.00 |
Refinement procedure
Resolution | 10.000 - 2.900 |
R-factor | 0.25 * |
Rwork | 0.237 |
R-free | 0.28000 * |
RMSD bond length | 0.009 |
RMSD bond angle | 1.140 * |
Data reduction software | DENZO |
Phasing software | RSREF |
Refinement software | CNS (0.9) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 18.000 | |
High resolution limit [Å] | 2.900 | |
Rmerge | 0.091 | |
Number of reflections | 38244 | |
Completeness [%] | 75.0 * | 55 * |
Redundancy | 1.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | MICRODIALYSIS | 6.8 | 315 | 2.0 M K2HPO4 , pH 6.8, MICRODIALYSIS, temperature 315K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | 1 | potassium phosphate | 2.0 (M) |