1SSD
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 | P 41 21 2 |
| Unit cell lengths | 88.422, 88.422, 161.874 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 19.700 - 2.900 |
| R-factor | 0.15794 |
| Rwork | 0.156 |
| R-free | 0.19287 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 8tim |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.188 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | REFMAC (5.1.24) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 19.730 | |
| High resolution limit [Å] | 2.900 | 2.900 |
| Rmerge | 0.105 | 0.298 |
| Number of reflections | 20217 | |
| <I/σ(I)> | 15.1 | 7.1 |
| Completeness [%] | 98.8 | 99.4 |
| Redundancy | 5.41 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5.5 | 294 | citrate, ammonium sulphate, sodium chloride, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 294K |
