1FT8
CRYSTAL STRUCTURE OF THE RNA-BINDING DOMAIN OF THE MRNA EXPORT FACTOR TAP
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-4 |
| Synchrotron site | ESRF |
| Beamline | ID14-4 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2000-02-03 |
| Detector | MARRESEARCH |
| Spacegroup name | P 41 21 2 |
| Unit cell lengths | 139.918, 139.918, 206.703 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 30.000 - 3.150 |
| R-factor | 0.303 |
| Rwork | 0.303 |
| R-free | 0.30300 |
| RMSD bond length | 0.015 |
| RMSD bond angle | 1.750 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | SHARP |
| Refinement software | CNS |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 3.250 |
| High resolution limit [Å] | 3.150 | 3.150 |
| Rmerge | 0.064 | 0.280 |
| Total number of observations | 227961 * | |
| Number of reflections | 35832 | |
| <I/σ(I)> | 11.6 | |
| Completeness [%] | 99.6 * | 99.9 |
| Redundancy | 6.4 | 6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion * | 6.8 | 4 * | drop consists of equal amounts of protein and reservoir solutions * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 20 (mg/ml) | |
| 2 | 1 | reservoir | cacodylate | 100 (mM) | |
| 3 | 1 | reservoir | PEG8000 | 18 (%(w/v)) | |
| 4 | 1 | reservoir | EDTA | 20 (mM) |
