5YBA
Dimeric Cyclophilin from T.vaginalis in complex with Myb1 peptide
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSRRC BEAMLINE BL13C1 |
| Synchrotron site | NSRRC |
| Beamline | BL13C1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2016-11-17 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.9762 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 37.785, 78.071, 117.708 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 29.448 - 2.062 |
| R-factor | 0.1722 |
| Rwork | 0.168 |
| R-free | 0.21290 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1dyw |
| RMSD bond length | 0.007 |
| RMSD bond angle | 0.895 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.10.1_2155) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 29.450 | 2.130 |
| High resolution limit [Å] | 2.060 | 2.060 |
| Rmerge | 0.543 | |
| Number of reflections | 22285 | |
| <I/σ(I)> | 9.81 | 2.039 |
| Completeness [%] | 91.0 | 90.3 |
| Redundancy | 5.3 | 3.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8 | 283 | 100 mM Tris-HCl pH 8.0, 30% (v/v) polyethylene glycol 400 |
