1H2V
Structure of the human nuclear cap-binding-complex (CBC)
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID14-2 |
Synchrotron site | ESRF |
Beamline | ID14-2 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2001-10-07 |
Detector | ADSC CCD |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 264.136, 59.605, 75.430 |
Unit cell angles | 90.00, 99.52, 90.00 |
Refinement procedure
Resolution | 19.670 - 2.000 |
R-factor | 0.212 |
Rwork | 0.212 |
R-free | 0.24700 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1h6k |
RMSD bond length | 0.006 |
RMSD bond angle | 19.400 * |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | MOLREP |
Refinement software | CNS (1.0) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 25.000 | 2.120 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.053 | 0.479 |
Number of reflections | 59304 * | |
<I/σ(I)> | 18.5 | 3.23 |
Completeness [%] | 79.5 | 58.8 |
Redundancy | 5.7 | 4.65 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 6 | 277 * | Mazza, C., (2002) Acta Crystallogr.,Sect.D, 58, 2194. * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 10 (mg/ml) | |
2 | 1 | reservoir | PEG6000 | 10 (%) | |
3 | 1 | reservoir | MES | 100 (mM) | pH6. |