1E1O
lysyl-tRNA Synthetase (LYSU) hexagonal form, complexed with lysine
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | EMBL/DESY, HAMBURG BEAMLINE BW7B |
| Synchrotron site | EMBL/DESY, HAMBURG |
| Beamline | BW7B |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 1995-06-15 |
| Detector | MARRESEARCH |
| Spacegroup name | P 61 2 2 |
| Unit cell lengths | 143.100, 143.100, 176.100 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 20.000 - 2.120 |
| R-factor | 0.195 |
| Rwork | 0.195 |
| R-free | 0.23300 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1lyl |
| RMSD bond length | 0.007 |
| RMSD bond angle | 23.700 * |
| Data reduction software | MOSFLM |
| Data scaling software | CCP4 |
| Phasing software | X-PLOR (3.1) |
| Refinement software | X-PLOR (3.1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 25.000 | 2.160 |
| High resolution limit [Å] | 2.120 | 2.120 |
| Rmerge | 0.085 | 0.260 |
| Total number of observations | 977338 * | |
| Number of reflections | 60434 | |
| <I/σ(I)> | 8.8 | 3.7 |
| Completeness [%] | 99.6 | 99.6 |
| Redundancy | 16.2 | 15.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 7.5 * | PROTEIN WAS CRYSTALLISED FROM 0.1M PIPES PH 6.8, 0.5 M LICL; 20% PEG 4K, 17% GLYCEROL |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 12 (mg/ml) | |
| 2 | 1 | drop | HEPES | 20 (mM) | |
| 3 | 1 | drop | lysine | 5 (mM) | |
| 4 | 1 | drop | beta-mercaptoethanol | 2 (mM) | |
| 5 | 1 | reservoir | PEG2000 | 20 (%) | |
| 6 | 1 | reservoir | 0.5 (M) | ||
| 7 | 1 | reservoir | PIPES | 0.1 (M) |
