1F3U
CRYSTAL STRUCTURE OF THE RAP30/74 INTERACTION DOMAINS OF HUMAN TFIIF
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID14-4 |
Synchrotron site | ESRF |
Beamline | ID14-4 |
Temperature [K] | 105 |
Detector technology | CCD |
Collection date | 1998-11-27 |
Detector | ADSC QUANTUM 4 |
Spacegroup name | P 1 |
Unit cell lengths | 48.015, 72.290, 82.266 |
Unit cell angles | 104.51, 93.32, 104.32 |
Refinement procedure
Resolution | 6.000 - 1.700 |
R-factor | 0.225 * |
Rwork | 0.225 |
R-free | 0.26000 |
RMSD bond length | 0.006 |
RMSD bond angle | 26.230 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | CNS (0.5) |
Refinement software | CNS (0.5) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 67.000 | 1.760 |
High resolution limit [Å] | 1.700 | 1.700 |
Rmerge | 0.065 | 0.194 |
Number of reflections | 108916 | |
<I/σ(I)> | 9.6 | |
Completeness [%] | 96.8 | 92.9 |
Redundancy | 2.2 | 1.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 4 * | PEG 1500, lithium nitrate, bis-Tris, DTT, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 278K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 5 (mg/ml) | |
2 | 1 | drop | PEG1500 | 13-15 (%) | |
3 | 1 | drop | 75 (mM) | ||
4 | 1 | drop | Bis-Tris | 32.5 (mM) | |
5 | 1 | drop | dithiothreitol | 1 (mM) | |
6 | 1 | reservoir | PEG1500 | 18-20 (%) | |
7 | 1 | reservoir | 100 (mM) | ||
8 | 1 | reservoir | Bis-Tris | 50 (mM) | |
9 | 1 | reservoir | dithiothreitol | 1 (mM) |