5TPT
The Crystal Structure of Amyloid Precursor-Like Protein 2 (APLP2) E2 Domain
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | AUSTRALIAN SYNCHROTRON BEAMLINE MX2 |
| Synchrotron site | Australian Synchrotron |
| Beamline | MX2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2013-06-07 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.95370 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 35.749, 150.118, 39.107 |
| Unit cell angles | 90.00, 109.69, 90.00 |
Refinement procedure
| Resolution | 37.529 - 2.422 |
| R-factor | 0.2184 |
| Rwork | 0.214 |
| R-free | 0.25950 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3umi |
| RMSD bond length | 0.004 |
| RMSD bond angle | 0.717 |
| Data reduction software | XDS |
| Data scaling software | Aimless (0.1.2) |
| Phasing software | MOLREP |
| Refinement software | PHENIX (1.9_1692) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 37.530 | 37.530 | 2.510 |
| High resolution limit [Å] | 2.420 | 8.830 | 2.420 |
| Rmerge | 0.136 | 0.030 | 0.841 |
| Rmeas | 0.148 | ||
| Rpim | 0.058 | ||
| Total number of observations | 94037 | ||
| Number of reflections | 14709 | ||
| <I/σ(I)> | 9.3 | ||
| Completeness [%] | 99.7 | 99.3 | 99.3 |
| Redundancy | 6.4 | 6.1 | 6.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 4.4 | 298.15 | 0.1 M phosphate-citrate, 40% PEG400 |
