8ANJ
Structure of the amyloid-forming peptide DFINWL from human GLP-2
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU PhotonJet-R |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2021-11-09 |
Detector | RIGAKU HyPix-6000HE |
Wavelength(s) | 1.54184 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 21.780, 4.869, 21.936 |
Unit cell angles | 90.00, 101.73, 90.00 |
Refinement procedure
Resolution | 16.950 - 1.550 |
R-factor | 0.1689 |
Rwork | 0.168 |
R-free | 0.17440 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | crystal structure of LYIQWL |
RMSD bond length | 0.011 |
RMSD bond angle | 0.956 |
Data reduction software | CrysalisPro |
Data scaling software | CrysalisPro |
Phasing software | MOLREP |
Refinement software | PHENIX (1.20.1_4487) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 16.960 | 1.610 |
High resolution limit [Å] | 1.550 | 1.550 |
Rmeas | 0.067 | 0.356 |
Number of reflections | 773 | 77 |
<I/σ(I)> | 12.1 | 2.2 |
Completeness [%] | 98.3 | 87.5 |
Redundancy | 2.88 | |
CC(1/2) | 0.999 | 0.921 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | EVAPORATION, RECRYSTALLIZATION | 310 | Lyophilized peptide was dissolved in 0.6 mg/ml concentration in a solution containing 30 % acetonitrile and 0.1 % TFA and incubated at 310K for 4 weeks. |