1IJF
Nucleotide exchange mechanisms in the eEF1A-eEF1Ba complex
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ELETTRA BEAMLINE 5.2R |
Synchrotron site | ELETTRA |
Beamline | 5.2R |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2000-07-13 |
Detector | MARRESEARCH |
Wavelength(s) | 1.00 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 64.247, 91.728, 92.713 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 13.990 - 3.000 |
R-factor | 0.25 |
Rwork | 0.250 |
R-free | 0.26000 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1f60 |
RMSD bond length | 0.008 |
RMSD bond angle | 1.800 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | CNS |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 14.000 | 3.110 |
High resolution limit [Å] | 3.000 | 3.000 |
Rmerge | 0.084 | 0.172 |
Number of reflections | 10905 | |
<I/σ(I)> | 19.8 | |
Completeness [%] | 99.1 | 91 |
Redundancy | 5.8 | 3.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7.2 * | 277 | Pedersen, L.P., (2000) Acta Crystallogr., D57, 159. * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 8 (mg/ml) | |
2 | 1 | drop | HEPES | 20 (mM) | |
3 | 1 | drop | 100 (mM) | ||
4 | 1 | drop | dithiothreitol | 0.5 (mM) | |
5 | 1 | reservoir | 100 (mM) | ||
6 | 1 | reservoir | Tris-HCl | 100 (mM) | |
7 | 1 | reservoir | dithiothreitol | 3 (mM) | |
8 | 1 | reservoir | PEG2000 MME | 15-18 (%) |