1GHE
CRYSTAL STRUCTURE OF TABTOXIN RESISTANCE PROTEIN COMPLEXED WITH AN ACYL COENZYME A
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 19-ID |
| Synchrotron site | APS |
| Beamline | 19-ID |
| Temperature [K] | 115 |
| Detector technology | CCD |
| Collection date | 2000-09-01 |
| Detector | SBC-2 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 101.760, 45.700, 84.240 |
| Unit cell angles | 90.00, 105.79, 90.00 |
Refinement procedure
| Resolution | 30.000 - 1.550 |
| Rwork | 0.209 |
| R-free | 0.23000 |
| RMSD bond length | 0.198 * |
| RMSD bond angle | 2.400 * |
| Data reduction software | DENZO (2000) |
| Data scaling software | SCALEPACK (2000) |
| Refinement software | CNS (1.0) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 100.000 | 1.450 |
| High resolution limit [Å] | 1.490 * | 1.400 |
| Rmerge | 0.071 * | 0.320 |
| Total number of observations | 307917 * | |
| Number of reflections | 56060 * | |
| <I/σ(I)> | 5.9 | |
| Completeness [%] | 92.0 * | 65 |
| Redundancy | 3 | 1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 8 | 291 | PEG 4000, sodium acetate, Tris-HCL, pH 8.0, HANGING DROP/VAPOR DIFFUSION, temperature 291.0K |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | Tris-HCl | 25 (mM) | pH8.0 |
| 2 | 1 | drop | 150 (mM) | ||
| 3 | 1 | drop | dithiothreitol | 5 (mM) | |
| 4 | 1 | drop | PMSF | 1 (mM) | |
| 5 | 1 | drop | sodium-EDTA | 0.2 (mM) | |
| 6 | 1 | drop | protein | 20-25 (mg/ml) | |
| 7 | 1 | reservoir | Tris-HCl | 100 (mM) | pH8.0 |
| 8 | 1 | reservoir | PEG4000 | 36 (%(w/v)) | |
| 9 | 1 | reservoir | 0.21 (M) |
