7KSF
Crystal structure of Prototype Foamy Virus Protease-Reverse Transcriptase (native)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | CHESS BEAMLINE F1 |
| Synchrotron site | CHESS |
| Beamline | F1 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2016-03-31 |
| Detector | DECTRIS PILATUS 6M |
| Wavelength(s) | 0.97601 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 228.210, 52.540, 75.430 |
| Unit cell angles | 90.00, 90.09, 90.00 |
Refinement procedure
| Resolution | 50.000 - 2.900 |
| R-factor | 0.2439 |
| Rwork | 0.225 |
| R-free | 0.25720 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 7kse |
| RMSD bond length | 0.004 |
| RMSD bond angle | 0.714 |
| Data reduction software | iMOSFLM |
| Data scaling software | Aimless |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.18.2_3874) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 3.080 |
| High resolution limit [Å] | 2.900 | 2.900 |
| Rmerge | 0.128 | 1.532 |
| Rmeas | 0.157 | 1.888 |
| Rpim | 0.089 | 1.089 |
| Number of reflections | 19435 | 2867 |
| <I/σ(I)> | 7.1 | 1 |
| Completeness [%] | 96.1 | 88.4 |
| Redundancy | 5.1 | 5.1 |
| CC(1/2) | 0.993 | 0.334 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6 | 293 | 50 mM KCl, 50 mM sodium cacodylate trihydrate pH 6.0, 12% PEG 8000, 1.0 mM spermine, 1.0 mM L-argininamide, 200 mM glycyglycine or glycylglycylglycine, 100 mM CaCl2 |






