1MT3
Crystal Structure of the Tricorn Interacting Factor Selenomethionine-F1
Experimental procedure
Experimental method | MAD |
Source type | SYNCHROTRON |
Source details | MPG/DESY, HAMBURG BEAMLINE BW6 |
Synchrotron site | MPG/DESY, HAMBURG |
Beamline | BW6 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2001-09-04 |
Detector | MARRESEARCH |
Wavelength(s) | 0.9788, 0.9795, 0.9500 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 51.968, 60.759, 80.678 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 20.000 - 2.000 |
R-factor | 0.285 |
Rwork | 0.255 |
R-free | 0.28000 |
Structure solution method | MAD |
RMSD bond length | 0.012 |
RMSD bond angle | 1.594 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | SHARP |
Refinement software | CNS |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 20.000 |
High resolution limit [Å] | 2.000 |
Rmerge | 0.064 |
Number of reflections | 33131 * |
<I/σ(I)> | 24.6 |
Completeness [%] | 99.0 * |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion * | 6 | 293 | 12% PEG 6000, 100 mM MES, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 20 (mg/ml) | |
2 | 1 | reservoir | MES | 100 (mM) | pH6.0 |
3 | 1 | reservoir | Bis-Tris-HCl | 100 (mM) | pH6.0 |
4 | 1 | reservoir | PEG6000 | 7-12 (%) | |
5 | 1 | reservoir | HEPES | 100 (mM) | pH7.5 |
6 | 1 | reservoir | PEG8000 | 20 (%) |