1SQ7
Understanding protein lids: Structural analysis of active hinge mutants in triosephosphate isomerase
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | EMBL/DESY, HAMBURG BEAMLINE X11 |
| Synchrotron site | EMBL/DESY, HAMBURG |
| Beamline | X11 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2002-06-15 |
| Detector | MARRESEARCH |
| Wavelength(s) | 0.8 |
| Spacegroup name | P 61 2 2 |
| Unit cell lengths | 61.670, 61.670, 500.886 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 28.280 - 2.850 |
| R-factor | 0.20468 |
| Rwork | 0.202 |
| R-free | 0.25185 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 8tim |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.074 |
| Data scaling software | XDS |
| Phasing software | AMoRE |
| Refinement software | REFMAC (5.1.24) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 2.930 |
| High resolution limit [Å] | 2.800 | 2.760 |
| Rmerge | 0.083 | 0.117 |
| Number of reflections | 15311 | |
| <I/σ(I)> | 10.42 | 7 |
| Completeness [%] | 94.3 | 82.4 |
| Redundancy | 6.62 | 5.29 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5.2 | 295 | PEG 6000, citrate, t-butanol, pH 5.2, VAPOR DIFFUSION, HANGING DROP, temperature 295K |
