6LT7
Crystal structure of human RPP20-RPP25 proteins in complex with the P3 domain of lncRNA RMRP
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SSRF BEAMLINE BL19U1 |
| Synchrotron site | SSRF |
| Beamline | BL19U1 |
| Temperature [K] | 93 |
| Detector technology | PIXEL |
| Collection date | 2016-07-15 |
| Detector | DECTRIS PILATUS3 6M |
| Wavelength(s) | 0.97776 |
| Spacegroup name | P 32 |
| Unit cell lengths | 144.168, 144.168, 74.223 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 35.600 - 2.700 |
| R-factor | 0.1938 |
| Rwork | 0.192 |
| R-free | 0.23850 |
| Structure solution method | SAD |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.813 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | SHELXCD |
| Refinement software | REFMAC (5.8.0232) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 2.750 |
| High resolution limit [Å] | 2.700 | 7.320 | 2.700 |
| Rmerge | 0.187 | 0.179 | 0.803 |
| Rmeas | 0.198 | 0.190 | 0.857 |
| Rpim | 0.062 | 0.063 | 0.293 |
| Total number of observations | 482821 | ||
| Number of reflections | 47259 | 2368 | 2380 |
| <I/σ(I)> | 4.1 | ||
| Completeness [%] | 100.0 | 100 | 99.7 |
| Redundancy | 10.2 | 10.2 | 8.1 |
| CC(1/2) | 0.920 | 0.833 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.6 | 277 | 20% of PEG 3350, 0.2 M ammonium tartrate dibasic, pH 6.6 |






