4OO6
Crystal structure of human KAP-beta2 bound to the NLS of HCC1 (Hepato Cellular Carcinoma protein 1)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSLS BEAMLINE X29A |
| Synchrotron site | NSLS |
| Beamline | X29A |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2013-03-20 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 1.0750 |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 126.584, 162.152, 68.501 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 40.000 - 2.700 |
| R-factor | 0.1912 |
| Rwork | 0.189 |
| R-free | 0.23840 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4fdd |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.440 |
| Data reduction software | XDS |
| Data scaling software | XDS |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0049) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 40.000 | 2.810 |
| High resolution limit [Å] | 2.700 | 2.700 |
| Rmerge | 0.102 | 1.295 |
| Number of reflections | 39520 | |
| <I/σ(I)> | 13.3 | 1.4 |
| Completeness [%] | 99.9 | 99.7 |
| Redundancy | 5.3 | 5.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6.25 | 298 | "Protein (20 MM HEPES, PH 7.3, 110 MM POTASSIUM ACETATE, 2MM MAGNESIUM ACET ATE, 20% GLYCEROL, 2MM DTT); Reservoir (0.2 M Sodiumchloride, 0.8M Sodiumcitrate, 0.1M BisTris pH 6.25 ); Cryo (2.5 M Sodiummalonate)">, VAPOR DIFFUSION, SITTING DROP, temperature 298K |






