1BBU
LYSYL-TRNA SYNTHETASE (LYSS) COMPLEXED WITH LYSINE
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SRS BEAMLINE PX9.6 |
Synchrotron site | SRS |
Beamline | PX9.6 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 1999-06-01 |
Detector | MARRESEARCH |
Spacegroup name | P 61 2 2 |
Unit cell lengths | 181.820, 181.820, 93.070 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 20.000 - 2.700 |
R-factor | 0.228 |
Rwork | 0.228 |
R-free | 0.29700 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1lyl |
RMSD bond length | 0.008 |
RMSD bond angle | 23.300 * |
Data reduction software | MOSFLM |
Data scaling software | CCP4 |
Phasing software | CCP4 |
Refinement software | X-PLOR (3.851) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 2.840 |
High resolution limit [Å] | 2.700 | 2.700 |
Rmerge | 0.071 | 0.222 |
Total number of observations | 87419 * | |
Number of reflections | 25113 | |
<I/σ(I)> | 6 | 3.2 |
Completeness [%] | 99.2 | 99.1 |
Redundancy | 3.5 | 3.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 8 * | 4 * | pH 7.5 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 20 (mg/ml) | |
2 | 1 | drop | Tris-HCl | 20 (mM) | |
3 | 1 | drop | 2-mercaptoethanol | 10 (mM) | |
4 | 1 | drop | 10 (mM) | ||
5 | 1 | reservoir | HEPES | 0.1 (M) | |
6 | 1 | reservoir | ammonium sulfate | 46-50 (%sat) | |
7 | 1 | reservoir | PEG400 | 2-4 (%) | |
8 | 1 | reservoir | glycerol | 15-20 (%) |