2J6C
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 | C 2 2 21 |
| Unit cell lengths | 82.770, 83.528, 33.989 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 58.820 - 1.300 |
| R-factor | 0.186 |
| Rwork | 0.185 |
| R-free | 0.21900 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.013 |
| RMSD bond angle | 1.391 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 1.580 |
| High resolution limit [Å] | 1.500 | 1.500 |
| Rmerge | 0.050 | 0.020 |
| Number of reflections | 16423 | |
| <I/σ(I)> | 19.2 | 3.9 |
| Completeness [%] | 91.2 | 79.3 |
| Redundancy | 59 | 5.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 8 | 25% PEG 4000, 0.1M NAAC, 0.1M TRIS-HCL PH 8.8 |
