1G6W
CRYSTAL STRUCTURE OF THE GLOBULAR REGION OF THE PRION PROTEIN URE2 FROM THE YEAST SACCAROMYCES CEREVISIAE
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-1 |
| Synchrotron site | ESRF |
| Beamline | ID14-1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 1999-12-14 |
| Detector | MARRESEARCH |
| Wavelength(s) | 0.934 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 54.680, 125.020, 159.950 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 20.000 - 2.500 |
| R-factor | 0.24 |
| Rwork | 0.210 |
| R-free | 0.26960 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.006 |
| RMSD bond angle | 1.248 |
| Data reduction software | DENZO |
| Data scaling software | CCP4 ((SCALA)) |
| Phasing software | AMoRE |
| Refinement software | CNS (1.0) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 2.640 |
| High resolution limit [Å] | 2.500 | 2.500 |
| Rmerge | 0.073 | 0.291 |
| Total number of observations | 277255 * | |
| Number of reflections | 36861 | |
| <I/σ(I)> | 5.7 | |
| Completeness [%] | 95.0 | 95 |
| Redundancy | 3.8 | 3.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 291 | PEG 4000, CaCl2 , pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 6 (mg/ml) | |
| 2 | 1 | reservoir | PEG4000 | 28 (%) | |
| 3 | 1 | reservoir | 260 (mM) | ||
| 4 | 1 | reservoir | Tris | 100 (mM) |
