7POK
Crystal structure of ZAD-domain of Pita protein from D.melanogaster
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SPRING-8 BEAMLINE BL41XU |
| Synchrotron site | SPring-8 |
| Beamline | BL41XU |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2017-06-29 |
| Detector | DECTRIS PILATUS 6M |
| Wavelength(s) | 1.0 |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 87.265, 90.489, 105.770 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 62.810 - 1.800 |
| R-factor | 0.1913 |
| Rwork | 0.190 |
| R-free | 0.22190 |
| Structure solution method | SAD |
| RMSD bond length | 0.017 |
| RMSD bond angle | 2.095 |
| Data reduction software | HKL-2000 |
| Data scaling software | Aimless (0.7.4) |
| Phasing software | CRANK2 (2.0.281) |
| Refinement software | REFMAC (5.8.0267) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 105.770 | 105.770 | 1.840 |
| High resolution limit [Å] | 1.800 | 9.000 | 1.800 |
| Rmerge | 0.051 | 0.027 | 1.195 |
| Rmeas | 0.056 | 0.030 | 1.308 |
| Rpim | 0.022 | 0.012 | 0.525 |
| Total number of observations | 240385 | 2096 | 13552 |
| Number of reflections | 38834 | 366 | 2262 |
| <I/σ(I)> | 14 | 85.4 | 0.5 |
| Completeness [%] | 99.4 | 99.6 | 98.9 |
| Redundancy | 6.2 | 5.7 | 6 |
| CC(1/2) | 0.999 | 0.999 | 0.730 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 277 | 0.1M HEPES pH 7.5, 20% PEG 10 000 |
