1OAI
Complex between Tap UBA domain and FxFG nucleoporin peptide
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE BM14 |
Synchrotron site | ESRF |
Beamline | BM14 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2002-04-15 |
Detector | ASCD |
Spacegroup name | P 31 2 1 |
Unit cell lengths | 42.974, 42.974, 66.852 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 6.000 - 1.000 |
Rwork | 0.149 |
R-free | 0.15800 * |
Structure solution method | MIRAS |
RMSD bond length | 0.023 * |
RMSD bond angle | 1.940 * |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | CCP4 |
Refinement software | REFMAC (5.1.24) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 25.000 * | 1.050 |
High resolution limit [Å] | 1.000 | 1.000 |
Rmerge | 0.065 | 0.357 * |
Total number of observations | 217401 * | |
Number of reflections | 39136 * | |
<I/σ(I)> | 5.334 | 1.92 |
Completeness [%] | 100.0 | 100 |
Redundancy | 5.6 * | 4.8 * |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 6.5 | 18 * | AS DESCRIBED IN MANUSCRIPT, pH 6.50 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | reservoir | ammonium acetate | 100 (mM) | pH6.5 |
2 | 1 | reservoir | ammonium sulfate | 1.9 (M) | |
3 | 1 | reservoir | dithiothreitol | 10 (mM) | |
4 | 1 | reservoir | EDTA | 1 (mM) | |
5 | 1 | drop | Tap UBA | 1.3 (mM) | |
6 | 1 | drop | FxFG peptide | 2.3 (mM) |