2X1U
Crystallographic binding studies with an engineered monomeric variant of triosephosphate isomerase
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | ENRAF-NONIUS FR591 |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2008-09-10 |
| Detector | MARRESEARCH |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 45.668, 85.381, 56.295 |
| Unit cell angles | 90.00, 98.85, 90.00 |
Refinement procedure
| Resolution | 8.220 - 1.840 |
| R-factor | 0.185 |
| Rwork | 0.183 |
| R-free | 0.23700 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2vek |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.020 |
| 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] | 16.230 | 1.890 |
| High resolution limit [Å] | 1.840 | 1.840 |
| Rmerge | 0.050 | 0.330 |
| Number of reflections | 36565 | |
| <I/σ(I)> | 13.5 | 3 |
| Completeness [%] | 97.9 | 99.4 |
| Redundancy | 2.7 | 2.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 5.5 | 20% PEG6000, 0.1M CITRATE, PH 5.5 |
