6AR1
Structure of a Thermostable Group II Intron Reverse Transcriptase with Template-Primer and Its Functional and Evolutionary Implications (RT/Duplex (Nat))
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 | 2016-11-12 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.9765 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 179.151, 95.052, 71.567 |
| Unit cell angles | 90.00, 113.55, 90.00 |
Refinement procedure
| Resolution | 47.530 - 3.010 |
| R-factor | 0.2184 |
| Rwork | 0.216 |
| R-free | 0.25470 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 6ar3 |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.170 |
| 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] | 47.530 | 47.530 | 3.190 |
| High resolution limit [Å] | 3.010 | 9.030 | 3.010 |
| Rmerge | 0.113 | 0.023 | 0.852 |
| Rmeas | 0.121 | 0.025 | 0.914 |
| Rpim | 0.044 | 0.009 | 0.330 |
| Total number of observations | 166560 | ||
| Number of reflections | 21941 | 839 | 3497 |
| <I/σ(I)> | 16.2 | ||
| Completeness [%] | 99.8 | 99.2 | 99.1 |
| Redundancy | 7.6 | 7.3 | 7.6 |
| CC(1/2) | 0.999 | 1.000 | 0.886 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 293 | Tris-HCl, sodium citrate tribasic dihydrate |
