1ESQ
CRYSTAL STRUCTURE OF THIAZOLE KINASE MUTANT (C198S) WITH ATP AND THIAZOLE PHOSPHATE.
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 | 1999-06-18 |
| Detector | APS |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 54.080, 100.840, 72.510 |
| Unit cell angles | 90.00, 95.10, 90.00 |
Refinement procedure
| Resolution | 20.000 - 2.500 |
| R-factor | 0.211 |
| Rwork | 0.209 |
| R-free | 0.28200 |
| RMSD bond length | 0.007 * |
| RMSD bond angle | 1.230 * |
| 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 | 2.590 |
| High resolution limit [Å] | 2.500 | 2.500 |
| Rmerge | 0.068 | 0.258 |
| Total number of observations | 111367 * | |
| Number of reflections | 26796 | |
| <I/σ(I)> | 7.9 | |
| Completeness [%] | 99.9 | 100 |
| Redundancy | 4.1 | 4 |
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)) |
