1SPQ
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 | 2003-02-10 |
| Detector | MARRESEARCH |
| Wavelength(s) | 0.8 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 80.706, 57.334, 106.154 |
| Unit cell angles | 90.00, 92.89, 90.00 |
Refinement procedure
| Resolution | 38.350 - 2.160 |
| R-factor | 0.16215 |
| Rwork | 0.160 |
| R-free | 0.19779 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 8tim |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.225 |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | REFMAC (5.1.24) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 40.000 | 2.210 |
| High resolution limit [Å] | 2.130 | 2.130 |
| Rmerge | 0.057 | 0.145 |
| Number of reflections | 25268 | |
| <I/σ(I)> | 22 | 7.4 |
| Completeness [%] | 97.8 | 78.8 |
| Redundancy | 3.48 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 9.1 | 277 | PEG 6000, Tris, 2-phosphoglycolate, pH 9.1, VAPOR DIFFUSION, HANGING DROP, temperature 277K |
