5AQ8
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 | 2011-11-24 |
| Detector | DECTRIS PILATUS 6M |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 41.070, 76.640, 106.450 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 43.717 - 1.620 |
| R-factor | 0.1887 |
| Rwork | 0.186 |
| R-free | 0.23520 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | PDB ENTRIES 3DTM AND 1SVX CHAIN A |
| RMSD bond length | 0.002 |
| RMSD bond angle | 0.658 |
| 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] | 43.720 | 1.680 |
| High resolution limit [Å] | 1.620 | 1.620 |
| Rmerge | 0.120 | |
| Number of reflections | 43423 | |
| <I/σ(I)> | 11.13 | 1.51 |
| Completeness [%] | 1.0 | 99.4 |
| Redundancy | 6.3 | 6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 7.5 | PEG4000 18.3 %, KSCN 0.286 M, HEPES-NA, 0.1 M, PH 7.5 |
