7TFQ
Crystal Structure of the Pirin Family Protein Redox-sensitive Bicupin YhaK Bound to Copper Ion from Yersinia pestis
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 | 2017-06-10 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.9796 |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 67.133, 100.737, 45.498 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 33.760 - 1.750 |
| R-factor | 0.167 |
| Rwork | 0.166 |
| R-free | 0.19560 |
| Structure solution method | SAD |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.042 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-3000 |
| Phasing software | HKL-3000 |
| Refinement software | PHENIX (1.19_4092) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.780 |
| High resolution limit [Å] | 1.750 | 1.750 |
| Rmerge | 0.081 | 0.676 |
| Number of reflections | 30621 | 1528 |
| <I/σ(I)> | 20.8 | 3.6 |
| Completeness [%] | 95.7 | 96.9 |
| Redundancy | 6.6 | 6.6 |
| CC(1/2) | 0.894 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 289 | 0.1 M Bis-Tris Propane pH 7, 35 %(w/v) tacsimate |
