2J6B
crystal structure of AFV3-109, a highly conserved protein from crenarchaeal viruses
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID14-1 |
Synchrotron site | ESRF |
Beamline | ID14-1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2006-02-15 |
Detector | ADSC QUANTUM 4 |
Spacegroup name | P 31 2 1 |
Unit cell lengths | 77.564, 77.564, 37.303 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 67.120 - 1.300 |
R-factor | 0.161 |
Rwork | 0.160 |
R-free | 0.19200 |
Structure solution method | SAD |
RMSD bond length | 0.009 |
RMSD bond angle | 1.420 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | SOLVE |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 1.330 |
High resolution limit [Å] | 1.300 | 1.300 |
Rmerge | 0.140 | 0.110 |
Number of reflections | 31813 | |
<I/σ(I)> | 13.1 | 2.8 |
Completeness [%] | 99.5 | 98.9 |
Redundancy | 9.9 | 8.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 4 | 30% PEG4000, 0.2M NAAC, PH 4 |