5AQA
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 | 2011-10-27 |
| Detector | DECTRIS PILATUS 6M |
| Spacegroup name | P 62 |
| Unit cell lengths | 163.120, 163.120, 66.760 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 47.089 - 2.600 |
| R-factor | 0.2292 |
| Rwork | 0.227 |
| R-free | 0.27520 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | PDB ENTRIES 3DTM AND 1SVX CHAIN A |
| RMSD bond length | 0.003 |
| RMSD bond angle | 0.628 |
| 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] | 47.000 | 2.690 |
| High resolution limit [Å] | 2.600 | 2.600 |
| Rmerge | 0.240 | |
| Number of reflections | 31359 | |
| <I/σ(I)> | 11.14 | 0.32 |
| Completeness [%] | 99.8 | 98 |
| Redundancy | 10 | 9.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 8 | PEG6000 17% W/V, AMMONIUM CHLORIDE 0.2 M, HEPES 0.05 M, PH 7.1 |
