4KML
Probing the N-terminal beta-sheet conversion in the crystal structure of the full-length human prion protein bound to a Nanobody
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SLS BEAMLINE X06DA |
Synchrotron site | SLS |
Beamline | X06DA |
Temperature [K] | 200 |
Detector technology | CCD |
Collection date | 2011-04-07 |
Detector | MARMOSAIC 225 mm CCD |
Wavelength(s) | 1.000 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 131.442, 45.921, 44.964 |
Unit cell angles | 90.00, 96.09, 90.00 |
Refinement procedure
Resolution | 31.610 - 1.500 |
R-factor | 0.17608 |
Rwork | 0.175 |
R-free | 0.19211 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2w9e |
RMSD bond length | 0.027 |
RMSD bond angle | 2.299 |
Data reduction software | HKL-3000 |
Data scaling software | SCALA |
Phasing software | PHASER |
Refinement software | REFMAC (5.7.0029) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 44.700 | 1.580 |
High resolution limit [Å] | 1.500 | 1.500 |
Number of reflections | 42289 | |
Completeness [%] | 96.9 | 97.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6 | 298 | A9 of the MD-proplex screen - 0.2 M sodium chloride, 0.1 M MES pH 6.0, 20% w/v PEG 2000 MME, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K |