2X2G
CRYSTALLOGRAPHIC BINDING STUDIES WITH AN ENGINEERED MONOMERIC VARIANT OF TRIOSEPHOSPHATE ISOMERASE
Replaces: 2X0MExperimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | ENRAF-NONIUS FR591 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2009-11-30 |
Detector | MAR scanner 345 mm plate |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 45.250, 85.790, 55.590 |
Unit cell angles | 90.00, 97.66, 90.00 |
Refinement procedure
Resolution | 14.073 - 1.900 |
R-factor | 0.1709 |
Rwork | 0.168 |
R-free | 0.22380 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2vek |
RMSD bond length | 0.007 |
RMSD bond angle | 1.071 |
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] | 15.000 | 1.950 |
High resolution limit [Å] | 1.900 | 1.900 |
Rmerge | 0.110 | 0.700 |
Number of reflections | 32859 | |
<I/σ(I)> | 13.5 | 2.9 |
Completeness [%] | 99.0 | 98.9 |
Redundancy | 3.6 | 3.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 5.5 | 20% PEG6000, 0.1M CITRATE, PH 5.5 |