5MJ6
Ligand-induced conformational change of Insulin-regulated aminopeptidase: insights on catalytic mechanism and active site plasticity.
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | DIAMOND BEAMLINE I03 |
Synchrotron site | Diamond |
Beamline | I03 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2014-12-06 |
Detector | DECTRIS PILATUS3 6M |
Wavelength(s) | 0.976 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 112.240, 143.170, 148.990 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 40.805 - 2.530 |
R-factor | 0.1766 |
Rwork | 0.174 |
R-free | 0.22920 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2yd0 |
RMSD bond length | 0.010 |
RMSD bond angle | 1.378 |
Data reduction software | xia2 |
Data scaling software | xia2 |
Phasing software | PHASER |
Refinement software | PHENIX (1.8.4_1496) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 40.805 | 2.600 |
High resolution limit [Å] | 2.530 | 2.530 |
Rmerge | 0.199 | |
Number of reflections | 80735 | |
<I/σ(I)> | 0.812 | 1.6 |
Completeness [%] | 100.0 | 100 |
Redundancy | 13.2 | 13.1 |
CC(1/2) | 0.997 | 0.451 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 291 | 18.8% (w/v) PEG of mean MW 20000, 37.6% (v/v) PEG monomethyl ether of mean MW 500, 50.2 mM Bicine, 43.8 mM Trizma base (pH of buffer mixture: 8.5) and 0.282 M each of the following halogens: Sodium fluoride, Sodium bromide and Sodium iodide |