3Q27
Cyrstal structure of human alpha-synuclein (32-57) fused to maltose binding protein (MBP)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 24-ID-C |
| Synchrotron site | APS |
| Beamline | 24-ID-C |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2010-07-24 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.97949 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 57.511, 49.951, 59.342 |
| Unit cell angles | 90.00, 92.19, 90.00 |
Refinement procedure
| Resolution | 59.299 - 1.302 |
| R-factor | 0.1323 |
| Rwork | 0.131 |
| R-free | 0.15590 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1anf |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.164 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER (2.1.4) |
| Refinement software | PHENIX (1.6.4_486) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 80.000 | 80.000 | 1.350 |
| High resolution limit [Å] | 1.300 | 2.800 | 1.300 |
| Rmerge | 0.078 | 0.050 | 0.568 |
| Number of reflections | 82058 | ||
| <I/σ(I)> | 16 | ||
| Completeness [%] | 99.6 | 96.1 | 99.9 |
| Redundancy | 6.2 | 6.2 | 5.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 9 | 290 | 0.1M bicine pH 9.0, 2.4 M ammonium sulfate, vapor diffusion, hanging drop, temperature 290K |
