5AQ9
DARPin-based Crystallization Chaperones exploit Molecular Geometry as a Screening Dimension in Protein Crystallography
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SLS BEAMLINE X06SA |
| Synchrotron site | SLS |
| Beamline | X06SA |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2012-06-02 |
| Detector | DECTRIS PILATUS 6M |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 41.480, 191.120, 219.510 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 48.047 - 1.860 |
| R-factor | 0.1827 |
| Rwork | 0.182 |
| R-free | 0.20380 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | PDB ENTRIES 3DTM AND 1SVX CHAINS A AND B |
| RMSD bond length | 0.003 |
| RMSD bond angle | 0.565 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | PHASER |
| Refinement software | PHENIX ((PHENIX.REFINE)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 47.780 | 1.930 |
| High resolution limit [Å] | 1.860 | 1.860 |
| Rmerge | 0.090 | |
| Number of reflections | 148199 | |
| <I/σ(I)> | 21.83 | 1.81 |
| Completeness [%] | 1.0 | 1 |
| Redundancy | 13.1 | 13.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 7.1 | PEG6000 17% W/V, AMMONIUM CHLORIDE 0.2 M, HEPES 0.05 M, PH 7.1 |
