7A9B
Crystal structure of Shank1 PDZ domain with ARAP3-derived peptide
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SLS BEAMLINE X06SA |
Synchrotron site | SLS |
Beamline | X06SA |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2019-03-01 |
Detector | DECTRIS EIGER X 16M |
Wavelength(s) | 0.999 |
Spacegroup name | P 61 2 2 |
Unit cell lengths | 67.799, 67.799, 248.967 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 47.932 - 2.000 |
R-factor | 0.203122312625 |
Rwork | 0.201 |
R-free | 0.24906 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1q3o |
RMSD bond length | 0.006 |
RMSD bond angle | 0.760 |
Data reduction software | XDS |
Data scaling software | Aimless |
Phasing software | PHASER |
Refinement software | PHENIX (1.10.1_2155) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 47.932 | 2.050 |
High resolution limit [Å] | 2.000 | 2.000 |
Number of reflections | 24047 | 1716 |
<I/σ(I)> | 12.2 | 2.2 |
Completeness [%] | 100.0 | 99.6 |
Redundancy | 9.2 | 9.5 |
CC(1/2) | 0.999 | 0.780 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 293 | 100 nL of protein solution (15 mg/ml mutant protein in 10 mM HEPES buffer, pH 8.0, 150 mM NaCl, 5% (v/v) glycerol and 0.5 mM TCEP) were mixed with 100 nL reservoir buffer (16% (w/v) polyethylene glycol 3350 and 0.2 M ammonium citrate), above a reservoir volume of 20 microL |