6PI7
Crystal structure of the TDRD2 extended Tudor domain in complex with an antibody fragment and the PIWIL1 peptide
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 19-ID |
| Synchrotron site | APS |
| Beamline | 19-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2012-08-16 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.97934 |
| Spacegroup name | P 63 |
| Unit cell lengths | 148.099, 148.099, 168.026 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 48.480 - 2.800 |
| R-factor | 0.1912 |
| Rwork | 0.190 |
| R-free | 0.20620 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3pnw |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.280 |
| Data reduction software | XDS |
| Data scaling software | Aimless (0.7.3) |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0238) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 48.480 | 48.480 | 2.890 |
| High resolution limit [Å] | 2.800 | 11.540 | 2.800 |
| Rmerge | 0.106 | 0.061 | 1.316 |
| Rmeas | 0.111 | 0.065 | 1.377 |
| Rpim | 0.033 | 0.020 | 0.404 |
| Total number of observations | 580022 | 6671 | 51128 |
| Number of reflections | 51311 | ||
| <I/σ(I)> | 16.6 | 32.8 | 1.8 |
| Completeness [%] | 99.8 | 89 | 100 |
| Redundancy | 11.3 | 9.7 | 11.6 |
| CC(1/2) | 0.998 | 0.997 | 0.565 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 293 | 20.0% (V/V) PEG 3350, 0.2 M tri- lithium citrate |
