1P69
STRUCTURAL BASIS FOR VARIATION IN ADENOVIRUS AFFINITY FOR THE CELLULAR RECEPTOR CAR (P417S MUTANT)
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | NSLS BEAMLINE X25 |
Synchrotron site | NSLS |
Beamline | X25 |
Temperature [K] | 99 |
Detector technology | CCD |
Detector | CUSTOM-MADE |
Wavelength(s) | 1.00 |
Spacegroup name | P 43 3 2 |
Unit cell lengths | 168.620, 168.620, 168.620 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 20.000 - 3.100 |
Rwork | 0.215 |
R-free | 0.25600 |
Structure solution method | MOLECULAR REPLACEMENT |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | CNS (1.0) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 3.210 |
High resolution limit [Å] | 3.100 | 3.100 |
Rmerge | 0.106 | |
Number of reflections | 14992 | |
Completeness [%] | 97.2 | 96.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | VAPOR DIFFUSION, SITTING DROP |