5EOQ
Structure of the murine Fab 1G6 bound to the vaccinia virus A27 peptide 31-40
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SSRL BEAMLINE BL11-1 |
| Synchrotron site | SSRL |
| Beamline | BL11-1 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2013-03-16 |
| Detector | PSI PILATUS 6M |
| Wavelength(s) | 0.976 |
| Spacegroup name | P 65 |
| Unit cell lengths | 99.339, 99.339, 117.564 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 49.670 - 1.950 |
| R-factor | 0.1993 |
| Rwork | 0.197 |
| R-free | 0.23520 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5eor |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.181 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.6.0104) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 49.670 | 2.060 |
| High resolution limit [Å] | 1.950 | 1.950 |
| Rmerge | 0.119 | 1.040 |
| Number of reflections | 45752 | |
| <I/σ(I)> | 12.3 | 2 |
| Completeness [%] | 95.7 | 96 |
| Redundancy | 4.2 | 7.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 295 | 20 % PEG 4000, 200 mM sodium phosphate dibasic |
