2J27
The functional role of the conserved active site proline of triosephosphate isomerase
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | EMBL/DESY, HAMBURG BEAMLINE BW7A |
| Synchrotron site | EMBL/DESY, HAMBURG |
| Beamline | BW7A |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2005-06-02 |
| Detector | MARRESEARCH |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 45.810, 97.320, 112.740 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 25.000 - 1.150 |
| R-factor | 0.1417 |
| R-free | 0.18950 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5tim |
| RMSD bond length | 0.013 |
| RMSD bond angle | 0.028 |
| Data reduction software | XDS |
| Data scaling software | XDS |
| Phasing software | MOLREP |
| Refinement software | SHELXL-97 |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 25.000 | 1.200 |
| High resolution limit [Å] | 1.150 | 1.150 |
| Rmerge | 0.060 | 0.350 |
| Number of reflections | 164758 | |
| <I/σ(I)> | 25.12 | 5.29 |
| Completeness [%] | 92.0 | 76.3 |
| Redundancy | 6.8 | 4.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 9.5 | WELL SOLUTION: 0.1 M CHES PH 9.5, 25 % PEG 1500, 200 MM MGSO4 PROTEIN SOLUTION: 11.5 MG/ML PROTEIN, 20 MM TRIS/HCL PH 7, 100 MM NACL, 1 MM DTT, 1 MM EDTA, 1 MM NAN3 AND 10 MM 2PG |
