5AQ7
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 | 2012-04-03 |
Detector | DECTRIS PILATUS 6M |
Spacegroup name | P 21 21 2 |
Unit cell lengths | 79.040, 156.240, 68.470 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 43.488 - 2.100 |
R-factor | 0.1919 |
Rwork | 0.190 |
R-free | 0.23000 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | PDB ENTRIES 3DTM AND 1SVX CHAIN A |
RMSD bond length | 0.003 |
RMSD bond angle | 0.714 |
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] | 43.490 | 2.180 |
High resolution limit [Å] | 2.100 | 2.100 |
Rmerge | 0.140 | |
Number of reflections | 50274 | |
<I/σ(I)> | 15.59 | 1.36 |
Completeness [%] | 99.9 | 99.3 |
Redundancy | 12 | 11.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 7.5 | PEG3350 20.0% W/V, SODIUM MALONATE 0.2 M, BIS TRIS PROPANE 0.1M, PH 7.5 |