1G6Y
CRYSTAL STRUCTURE OF THE GLOBULAR REGION OF THE PRION PROTEIN URE2 FROM YEAST SACCHAROMYCES 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 | 2000-02-24 |
| Detector | MARRESEARCH |
| Wavelength(s) | 0.934 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 54.490, 73.700, 130.970 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 20.000 - 2.800 |
| R-factor | 0.217 * |
| Rwork | 0.218 |
| R-free | 0.29290 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.360 |
| 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 | 2.900 |
| High resolution limit [Å] | 2.800 | 2.800 |
| Rmerge | 0.091 | 0.341 |
| Total number of observations | 170419 * | |
| Number of reflections | 12931 | |
| <I/σ(I)> | 8.8 | |
| Completeness [%] | 98.5 | 89.8 |
| Redundancy | 4 | 3.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 291 | Peg 1000, CaCl2, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 18K |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 5 (mg/ml) | |
| 2 | 1 | reservoir | PEG1000 | 30 (%) | |
| 3 | 1 | reservoir | 160 (mM) | ||
| 4 | 1 | reservoir | Tris | 100 (mM) |
