5HUY
Structure of HCMV Small Terminase NLS bound to importin alpha
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 21-ID-F |
| Synchrotron site | APS |
| Beamline | 21-ID-F |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2015-11-12 |
| Detector | MARMOSAIC 225 mm CCD |
| Wavelength(s) | 0.978 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 77.254, 90.810, 96.934 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 14.934 - 1.979 |
| R-factor | 0.1741 |
| Rwork | 0.173 |
| R-free | 0.19590 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3q5u |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.041 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | PHENIX ((1.10.1_2155: ???)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.020 |
| High resolution limit [Å] | 1.950 | 1.950 |
| Rmerge | 0.749 | |
| Number of reflections | 50602 | |
| <I/σ(I)> | 48.1 | 3.8 |
| Completeness [%] | 99.5 | 99.5 |
| Redundancy | 4.8 | 4.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6 | 293 | 2.3 uL of deltaIBB-importin alpha concentrated to 20 mg/ml were mixed with 0.7 microlitre of a 2-fold molar excess of HCMV-NLS peptide; 3 uL of reservoir solution containing ~0.7 M sodium citrate, 100 mM Hepes, and 10 mM beta-mercaptoethanol were added to the drop, pH 6.0 |
