3F62
Crystal Structure of Human IL-18 in complex with Ectromelia virus IL-18 Binding Protein
Experimental procedure
Experimental method | SAD |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 19-ID |
Synchrotron site | APS |
Beamline | 19-ID |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2004-04-03 |
Detector | BRUKER SMART 6500 |
Wavelength(s) | 0.97921 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 36.356, 69.210, 104.832 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 34.610 - 2.000 |
R-factor | 0.19089 |
Rwork | 0.189 |
R-free | 0.23545 |
RMSD bond length | 0.013 |
RMSD bond angle | 1.377 |
Data reduction software | HKL-3000 |
Data scaling software | HKL-3000 |
Phasing software | SHELXS |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.048 |
High resolution limit [Å] | 2.000 | 2.000 |
Number of reflections | 17333 | |
<I/σ(I)> | 12.66 | 1.5 |
Completeness [%] | 94.4 | 100 |
Redundancy | 5.4 | 4.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION | 7.5 | 298 | 30% Peg 3350, 0.5M KCl, 0.1M Sodium Citrate, pH 4.5, pH 7.5, VAPOR DIFFUSION, temperature 298K |