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 |
