5D5N
Crystal Structure of the Human Cytomegalovirus pUL50-pUL53 Complex
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | BESSY BEAMLINE 14.1 |
Synchrotron site | BESSY |
Beamline | 14.1 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2015-05-30 |
Detector | PSI PILATUS 6M |
Wavelength(s) | 0.9184 |
Spacegroup name | P 6 |
Unit cell lengths | 118.153, 118.153, 73.623 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 46.080 - 2.440 |
R-factor | 0.22566 |
Rwork | 0.221 |
R-free | 0.28717 |
Structure solution method | SAD |
RMSD bond length | 0.010 |
RMSD bond angle | 1.413 |
Data reduction software | XDS (XDSAPP) |
Data scaling software | XDS (XDSAPP) |
Phasing software | SHELX |
Refinement software | REFMAC (5.8.0107) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.500 |
High resolution limit [Å] | 2.440 | 2.440 |
Number of reflections | 20319 | |
<I/σ(I)> | 13.5 | 1.3 |
Completeness [%] | 99.9 | 99.9 |
Redundancy | 6.8 | 6.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 8 | 293 | Protein concentration: 10-13 mg/ml Protein buffer: 50 mM Tris/HCl pH 8.0, 150 mM NaCl, 2 mM TCEP Reservoir solution: 0.2 mM CaCl2, 20 % (w/v) PEG 3350 Ratio: 1:1 protein:reservoir solution |