2J24
The functional role of the conserved active site proline 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 | 2004-08-16 |
Detector | MAR scanner 345 mm plate |
Spacegroup name | P 1 |
Unit cell lengths | 37.500, 43.720, 71.270 |
Unit cell angles | 80.49, 79.61, 64.66 |
Refinement procedure
Resolution | 19.210 - 2.100 |
R-factor | 0.153 |
Rwork | 0.149 |
R-free | 0.23000 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 5tim |
RMSD bond length | 0.017 |
RMSD bond angle | 1.638 |
Data reduction software | XDS |
Data scaling software | XDS |
Phasing software | MOLREP |
Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 25.000 | 2.200 |
High resolution limit [Å] | 2.100 | 2.100 |
Rmerge | 0.070 | 0.130 |
Number of reflections | 22102 | |
<I/σ(I)> | 13.8 | 8.67 |
Completeness [%] | 94.5 | 92.2 |
Redundancy | 2.65 | 2.63 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 7 | WELL SOLUTION: 0.1 M TEA PH 7.0, 27% PEG 2K MME AND 0.2 M KSCN PROTEIN SOLUTION: 11 MG/ML PROTEIN, 0.02 M TRIS/HCL PH 7.0, 0.1 M NACL, 1 MM DTT, 1 MM EDTA AND 1 MM NAN3. |