3SV1
Crystal structure of APP peptide bound rat Mint2 PARM
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SSRF BEAMLINE BL17U |
Synchrotron site | SSRF |
Beamline | BL17U |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2011-04-23 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 0.9792 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 151.119, 52.092, 121.282 |
Unit cell angles | 90.00, 127.80, 90.00 |
Refinement procedure
Resolution | 40.700 - 3.300 |
R-factor | 0.243 |
Rwork | 0.243 |
R-free | 0.30100 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3suz |
RMSD bond length | 0.008 |
RMSD bond angle | 1.400 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHASER |
Refinement software | CNS (1.2) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 40.700 | 3.420 |
High resolution limit [Å] | 3.300 | 3.300 |
Number of reflections | 10867 | |
Completeness [%] | 94.5 | 94.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 293 | 0.1M HEPES, 36% PEG200, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K |