1ESJ
CRYSTAL STRUCTURE OF THIAZOLE KINASE MUTANT (C198S)
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 19-ID |
Synchrotron site | APS |
Beamline | 19-ID |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 1999-06-17 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 53.060, 100.890, 73.070 |
Unit cell angles | 90.00, 96.02, 90.00 |
Refinement procedure
Resolution | 20.000 - 1.800 |
R-factor | 0.23 |
Rwork | 0.229 |
R-free | 0.25300 |
RMSD bond length | 0.005 |
RMSD bond angle | 21.910 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | CNS |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 1.760 |
High resolution limit [Å] | 1.700 | 1.700 |
Rmerge | 0.042 | 0.375 |
Total number of observations | 340088 * | |
Number of reflections | 83184 | |
<I/σ(I)> | 9.6 | |
Completeness [%] | 98.6 | 93.6 |
Redundancy | 4.1 | 3.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, sitting drop * | 8.6 * | 291 | drop consists of equal volume of protein and reservoir solutions * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 30 (mg/ml) | |
2 | 1 | drop | Thz | 0.05 (mM) | |
3 | 1 | drop | ATP | 0.05 (mM) | |
4 | 1 | drop | 0.1 (mM) | ||
5 | 1 | reservoir | Tris-HCl | 100 (mM) | |
6 | 1 | reservoir | PEG8000 | 20 (%(w/v)) |