6QFU
Human carbonic anhydrase II with bound IrCp* complex (cofactor 7) to generate an artificial transfer hydrogenase (ATHase)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SLS BEAMLINE X06DA |
| Synchrotron site | SLS |
| Beamline | X06DA |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2018-10-31 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 1.000 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 42.038, 41.264, 71.900 |
| Unit cell angles | 90.00, 104.27, 90.00 |
Refinement procedure
| Resolution | 40.770 - 1.800 |
| R-factor | 0.166 |
| Rwork | 0.165 |
| R-free | 0.18640 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3zp9 |
| RMSD bond length | 0.013 |
| RMSD bond angle | 2.665 |
| Data reduction software | DIALS |
| Data scaling software | Aimless |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0238) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 40.770 | 1.850 |
| High resolution limit [Å] | 1.800 | 1.800 |
| Rmerge | 0.198 | 1.026 |
| Number of reflections | 21112 | 1553 |
| <I/σ(I)> | 10.3 | 7 |
| Completeness [%] | 99.3 | 99.9 |
| Redundancy | 8 | 8.5 |
| CC(1/2) | 0.958 | 0.386 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.9 | 293 | 2.6 M ammonium sulfate, 50 mM Tris-H2SO4 |
