2X1T
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 X12 |
Synchrotron site | EMBL/DESY, HAMBURG |
Beamline | X12 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2009-04-17 |
Detector | MARMOSAIC 225 mm CCD |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 45.640, 86.850, 55.880 |
Unit cell angles | 90.00, 97.33, 90.00 |
Refinement procedure
Resolution | 26.400 - 1.830 |
R-factor | 0.1741 |
Rwork | 0.172 |
R-free | 0.21940 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2vek |
RMSD bond length | 0.007 |
RMSD bond angle | 1.015 |
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] | 46.700 | 1.880 |
High resolution limit [Å] | 1.830 | 1.830 |
Rmerge | 0.060 | 0.460 |
Number of reflections | 38001 | |
<I/σ(I)> | 18.4 | 3 |
Completeness [%] | 99.7 | 99.6 |
Redundancy | 3.8 | 3.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 5.5 | 20% PEG6000, 0.1M CITRATE, PH 5.5 |