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 |
