4N9O
Probing the N-terminal beta-sheet conversion in the crystal structure of the human prion protein bound to a Nanobody
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE BM30A |
Synchrotron site | ESRF |
Beamline | BM30A |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2010-07-22 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 1.0000 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 131.857, 45.781, 45.092 |
Unit cell angles | 90.00, 96.23, 90.00 |
Refinement procedure
Resolution | 24.930 - 1.500 |
R-factor | 0.1514 |
Rwork | 0.150 |
R-free | 0.18430 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2w9e |
RMSD bond length | 0.023 |
RMSD bond angle | 1.939 |
Data reduction software | MOSFLM |
Data scaling software | SCALA (3.3.16) |
Phasing software | PHASER (2.1.4) |
Refinement software | REFMAC |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 65.540 | 25.185 | 1.580 |
High resolution limit [Å] | 1.500 | 4.740 | 1.500 |
Rmerge | 0.047 | 0.240 | |
Total number of observations | 5636 | 24907 | |
Number of reflections | 42399 | ||
<I/σ(I)> | 13.8 | 9.5 | 2.8 |
Completeness [%] | 98.8 | 98.1 | 97.8 |
Redundancy | 4 | 4 | 4.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7 | 298 | 0.1 M HEPES-Na pH 7, 15% PEG20000, VAPOR DIFFUSION, SITTING DROP, temperature 298K |