6K9X
Crystal Structure Analysis of Protein
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SSRF BEAMLINE BL19U1 |
| Synchrotron site | SSRF |
| Beamline | BL19U1 |
| Temperature [K] | 80 |
| Detector technology | CCD |
| Collection date | 2018-11-07 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 1.0 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 48.597, 58.268, 70.239 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 39.964 - 1.200 |
| R-factor | 0.1304 |
| Rwork | 0.130 |
| R-free | 0.14120 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2dfc |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.110 |
| Data reduction software | XDS |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.11.1_2575) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 39.964 | 1.243 |
| High resolution limit [Å] | 1.200 | 1.200 |
| Number of reflections | 62650 | 6177 |
| <I/σ(I)> | 18.32 | |
| Completeness [%] | 99.2 | |
| Redundancy | 5.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | EVAPORATION | 6 | 291 | PEG 8000, NaI, MES |






