2X16
Crystallographic binding studies with an engineered monomeric variant of triosephosphate isomerase
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | EMBL/DESY, HAMBURG BEAMLINE X11 |
Synchrotron site | EMBL/DESY, HAMBURG |
Beamline | X11 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2009-04-17 |
Detector | MAR555 FLAT PANEL |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 45.490, 85.300, 55.880 |
Unit cell angles | 90.00, 98.60, 90.00 |
Refinement procedure
Resolution | 44.979 - 2.130 |
R-factor | 0.1844 |
Rwork | 0.180 |
R-free | 0.26080 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2vek |
RMSD bond length | 0.007 |
RMSD bond angle | 1.050 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | MOLREP |
Refinement software | PHENIX ((PHENIX.REFINE)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 44.980 | 2.190 |
High resolution limit [Å] | 2.130 | 2.130 |
Rmerge | 0.070 | 0.470 |
Number of reflections | 23310 | |
<I/σ(I)> | 14.3 | 3 |
Completeness [%] | 98.4 | 97.6 |
Redundancy | 3.6 | 3.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 5.5 | 20% PEG6000, 0.1M CITRATE PH 5.5 |