3G7W
Islet Amyloid Polypeptide (IAPP or Amylin) Residues 1 to 22 fused to Maltose Binding Protein
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 | 2008-02-25 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 0.98085 |
Spacegroup name | P 41 21 2 |
Unit cell lengths | 84.495, 84.495, 144.292 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 55.220 - 1.750 |
R-factor | 0.171 |
Rwork | 0.170 |
R-free | 0.19400 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1mpd |
RMSD bond length | 0.009 |
RMSD bond angle | 1.193 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | PHASER |
Refinement software | REFMAC (5.5.0070) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 90.000 | 90.000 | 1.890 |
High resolution limit [Å] | 1.750 | 2.990 | 1.750 |
Rmerge | 0.099 | 0.097 | 0.431 |
Number of reflections | 53547 | ||
<I/σ(I)> | 16.958 | ||
Completeness [%] | 99.8 | 99 | 100 |
Redundancy | 12.3 | 11.8 | 12 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 4.6 | 298 | 2.0 M Ammonium Sulfate, 0.1M Sodium Acetate pH 4.6, vapor diffusion, hanging drop, temperature 298K |