2X1R
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 |
Detector | MAR555 FLAT PANEL |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 45.940, 86.920, 56.280 |
Unit cell angles | 90.00, 98.58, 90.00 |
Refinement procedure
Resolution | 14.920 - 1.980 |
R-factor | 0.164 |
Rwork | 0.161 |
R-free | 0.22600 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2vek |
RMSD bond length | 0.007 |
RMSD bond angle | 1.002 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | MOLREP |
Refinement software | PHENIX ((PHENIX.REFINE: 1.5_2)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 45.460 | 2.050 |
High resolution limit [Å] | 1.970 | 1.980 |
Rmerge | 0.090 | 0.430 |
Number of reflections | 28367 | |
<I/σ(I)> | 13.1 | 3 |
Completeness [%] | 91.4 | 85.1 |
Redundancy | 4.2 | 3.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 5.5 | 20% PEG6000, 0.1M CITRATE, PH 5.5 |