3PMR
Crystal Structure of E2 domain of Human Amyloid Precursor-Like Protein 1
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSLS BEAMLINE X29A |
| Synchrotron site | NSLS |
| Beamline | X29A |
| Wavelength(s) | 1.075 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 74.885, 81.269, 89.670 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 39.260 - 2.110 |
| R-factor | 0.2113 |
| Rwork | 0.208 |
| R-free | 0.24360 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.062 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 40.000 | 2.180 |
| High resolution limit [Å] | 2.100 | 2.100 |
| Rmerge | 0.070 | 0.402 |
| Number of reflections | 32194 | |
| <I/σ(I)> | 16.5 | |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 9.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 5.6 | 298 | 1.4M Na/K Phosphate, pH 5.6, VAPOR DIFFUSION, SITTING DROP, temperature 298K |
