4IM8
low resolution crystal structure of mouse RAGE
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 22-ID |
Synchrotron site | APS |
Beamline | 22-ID |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2012-08-04 |
Detector | MARMOSAIC 300 mm CCD |
Wavelength(s) | 1. |
Spacegroup name | P 41 3 2 |
Unit cell lengths | 115.810, 115.810, 115.810 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 23.162 - 3.503 |
R-factor | 0.2624 |
Rwork | 0.258 |
R-free | 0.33610 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3cjj |
RMSD bond length | 0.016 |
RMSD bond angle | 1.756 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHASER |
Refinement software | PHENIX ((phenix.refine: 1.8.1_1168)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 3.630 |
High resolution limit [Å] | 3.500 | 3.500 |
Number of reflections | 3672 | |
<I/σ(I)> | 8.1 | 4 |
Completeness [%] | 99.5 | 100 |
Redundancy | 13.1 | 12.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 298 | 0.1M Tris pH 8.5, 200mM MgCl2 and 22% PEG 400. Protein was purified on gel filtration in the presence of excess dodecasaccharide heparan sulfate that caused a shift in the elution profile from monomer to hexamer, VAPOR DIFFUSION, HANGING DROP, temperature 298K |