6AR3
Structure of a Thermostable Group II Intron Reverse Transcriptase with Template-Primer and Its Functional and Evolutionary Implications (RT/Duplex (Se-Met))
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ALS BEAMLINE 5.0.3 |
| Synchrotron site | ALS |
| Beamline | 5.0.3 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2016-06-12 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.9765 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 179.527, 108.966, 72.517 |
| Unit cell angles | 90.00, 113.78, 90.00 |
Refinement procedure
| Resolution | 48.930 - 3.410 |
| R-factor | 0.2783 |
| Rwork | 0.273 |
| R-free | 0.32370 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3kyl 5irf |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.258 |
| Data reduction software | XDS (May 1, 2016) |
| Data scaling software | Aimless (0.5.31) |
| Phasing software | PHASER (2.7.16) |
| Refinement software | REFMAC (5.8.0158) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 48.930 | 48.930 | 3.690 |
| High resolution limit [Å] | 3.410 | 9.030 | 3.410 |
| Rmerge | 0.224 | 0.039 | 0.850 |
| Rmeas | 0.240 | 0.042 | 0.912 |
| Rpim | 0.087 | 0.016 | 0.330 |
| Total number of observations | 132418 | ||
| Number of reflections | 17494 | 977 | 3571 |
| <I/σ(I)> | 9.2 | ||
| Completeness [%] | 99.9 | 99.5 | 99.7 |
| Redundancy | 7.6 | 7.1 | 7.6 |
| CC(1/2) | 0.995 | 0.999 | 0.884 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 293 | Tris-HCl, sodium citrate tribasic dihydrate |
