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 |