3RLK
Crystal structure of the read-through domain from bacteriophage Qbeta A1 protein, monoclinic crystal form
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID29 |
| Synchrotron site | ESRF |
| Beamline | ID29 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2009-03-05 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.976180 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 44.010, 49.120, 44.260 |
| Unit cell angles | 90.00, 118.41, 90.00 |
Refinement procedure
| Resolution | 38.930 - 1.760 |
| R-factor | 0.1768 |
| Rwork | 0.174 |
| R-free | 0.24180 |
| Structure solution method | MIRAS |
| RMSD bond length | 0.023 |
| RMSD bond angle | 1.925 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA (3.3.9) |
| Phasing software | SHARP |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 38.930 | 38.930 | 1.860 |
| High resolution limit [Å] | 1.760 | 5.570 | 1.760 |
| Rmerge | 0.046 | 0.334 | |
| Total number of observations | 1874 | 7776 | |
| Number of reflections | 16414 | ||
| <I/σ(I)> | 10 | 13.4 | 2.2 |
| Completeness [%] | 99.2 | 99.7 | 99.5 |
| Redundancy | 3.4 | 3.4 | 3.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 298 | 0.1 M Tris-HCl, 40% PEG 300, pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 298K |
