2ONX
NNQQ peptide corresponding to residues 8-11 of yeast prion sup35 (alternate crystal form)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID13 |
| Synchrotron site | ESRF |
| Beamline | ID13 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2005-07-16 |
| Detector | MAR CCD 165 mm |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 4.854, 16.014, 15.546 |
| Unit cell angles | 90.00, 96.91, 90.00 |
Refinement procedure
| Resolution | 15.430 - 1.520 |
| R-factor | 0.175 |
| Rwork | 0.172 |
| R-free | 0.20200 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1yjp |
| RMSD bond length | 0.013 |
| RMSD bond angle | 1.314 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 90.000 | 90.000 | 1.620 |
| High resolution limit [Å] | 1.500 | 2.560 | 1.500 |
| Rmerge | 0.152 | 0.101 | 0.299 |
| Number of reflections | 259 | ||
| <I/σ(I)> | 10.1 | ||
| Completeness [%] | 63.8 | 83.3 | 26.1 |
| Redundancy | 1.5 | 1.9 | 1.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5.6 | 298 | 30-50 mg/mL peptide disolved in water and mixed with an equal volume of reservoir solution consisting of 100 mM trisodium citrate, 20% polyethylene glycol 4000 and 20% isopropanol, pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
