8UC5
Apo X-ray crystal structure of Cyclophilin D with a surface entropy reduction mutation (K175I)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSLS-II BEAMLINE 17-ID-1 |
| Synchrotron site | NSLS-II |
| Beamline | 17-ID-1 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2022-02-02 |
| Detector | DECTRIS EIGER X 9M |
| Wavelength(s) | 0.9201 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 123.667, 56.643, 101.172 |
| Unit cell angles | 90.00, 123.72, 90.00 |
Refinement procedure
| Resolution | 29.330 - 1.430 |
| R-factor | 0.1448 |
| Rwork | 0.144 |
| R-free | 0.17540 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.122 |
| Data reduction software | XDS |
| Data scaling software | Aimless |
| Phasing software | DIMPLE |
| Refinement software | PHENIX (1.18rc7_3834) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 29.330 | 1.470 |
| High resolution limit [Å] | 1.430 | 1.430 |
| Rmeas | 0.093 | 0.807 |
| Number of reflections | 105128 | 7331 |
| <I/σ(I)> | 8.8 | 1.5 |
| Completeness [%] | 97.6 | 92.3 |
| Redundancy | 3.8 | 3.6 |
| CC(1/2) | 0.997 | 0.657 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7 | 293 | Well solution: 2.1 M DL-Malic acid pH 7.0. Protein solution: 15 mg/mL protein, 20 mM Tris pH 8.0, 50 mM NaCl, 1 mM DTT, and 5% glycerol. Drop: 1 uL protein, 1 uL well solution |
