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 |
