3RLC
Crystal structure of the read-through domain from bacteriophage Qbeta A1 protein, hexagonal crystal form
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | MAX II BEAMLINE I911-2 |
| Synchrotron site | MAX II |
| Beamline | I911-2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2011-02-17 |
| Detector | MAR CCD 165 mm |
| Wavelength(s) | 1.03874 |
| Spacegroup name | P 63 2 2 |
| Unit cell lengths | 69.110, 69.110, 167.300 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 29.930 - 2.900 |
| R-factor | 0.2166 |
| Rwork | 0.213 |
| R-free | 0.29690 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.368 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA (3.3.16) |
| Phasing software | MOLREP |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 34.555 | 34.555 | 3.060 |
| High resolution limit [Å] | 2.900 | 9.170 | 2.900 |
| Rmerge | 0.029 | 0.543 | |
| Total number of observations | 1726 | 7941 | |
| Number of reflections | 5773 | ||
| <I/σ(I)> | 17.5 | 18.8 | 1.4 |
| Completeness [%] | 100.0 | 98.6 | 100 |
| Redundancy | 9.5 | 7.3 | 10 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8 | 298 | 40% PEG 300, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 298K |
