2X1S
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 | 2009-12-01 |
| Detector | MARRESEARCH |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 45.820, 86.170, 56.280 |
| Unit cell angles | 90.00, 98.30, 90.00 |
Refinement procedure
| Resolution | 14.890 - 1.930 |
| R-factor | 0.162 |
| Rwork | 0.161 |
| R-free | 0.20100 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2vek |
| RMSD bond length | 0.006 |
| RMSD bond angle | 1.028 |
| 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] | 15.000 | 2.000 |
| High resolution limit [Å] | 1.920 | 1.920 |
| Rmerge | 0.100 | 0.390 |
| Number of reflections | 32518 | |
| <I/σ(I)> | 15.6 | 4.1 |
| Completeness [%] | 98.4 | 86.2 |
| Redundancy | 5.6 | 4.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 5.5 | 20% PEG6000, 0.1M CITRATE, PH 5.5 |
