4ZNN
MicroED structure of the segment, GVVHGVTTVA, from the A53T familial mutant of Parkinson's disease protein, alpha-synuclein residues 47-56
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ELECTRON MICROSCOPE |
| Source details | OTHER |
| Temperature [K] | 100 |
| Detector technology | CMOS |
| Collection date | 2015-04-20 |
| Wavelength(s) | 0.0251 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 17.930, 4.710, 33.030 |
| Unit cell angles | 90.00, 94.33, 90.00 |
Refinement procedure
| Resolution | 16.470 - 1.410 |
| R-factor | 0.2396 |
| Rwork | 0.235 |
| R-free | 0.28170 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | Ideal model |
| RMSD bond length | 0.020 |
| RMSD bond angle | 1.977 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | PHASER (2.5.6) |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 16.500 | 16.500 | 1.480 |
| High resolution limit [Å] | 1.410 | 4.680 | 1.410 |
| Rmerge | 0.236 | 0.078 | 0.780 |
| Rmeas | 0.264 | 0.100 | 0.895 |
| Total number of observations | 4110 | ||
| Number of reflections | 1120 | 36 | 100 |
| <I/σ(I)> | 4.62 | 7.18 | 1.08 |
| Completeness [%] | 86.9 | 87.8 | 58.5 |
| Redundancy | 3.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | BATCH MODE | 7 | 310 | 1 mg of synthetic peptide GVVHGVTTVA was dissolved in 200 microliters of 50 mM phosphate buffer pH 7.0 and 0.1% w/v DMSO and shaken overnight in an orbital mixing plate |
