2OLX
Structure of NNQQ Peptide from Yeast Prion SUP35
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 | 2005-12-19 |
Detector | MAR CCD 165 mm |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 15.479, 4.915, 30.552 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 15.280 - 1.420 |
R-factor | 0.188 |
Rwork | 0.183 |
R-free | 0.23500 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | polyalanine ideal beta-strand |
RMSD bond length | 0.008 |
RMSD bond angle | 1.397 |
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 | 1.450 |
High resolution limit [Å] | 1.400 | 3.020 | 1.400 |
Rmerge | 0.124 | 0.097 | 0.209 |
Number of reflections | 426 | ||
<I/σ(I)> | 8.7 | ||
Completeness [%] | 74.9 | 97.3 | 54.3 |
Redundancy | 3.1 | 3 | 2.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 298 | VAPOR DIFFUSION, HANGING DROP, temperature 298K |