6VWU
X-ray structure of ALKS 4230, a fusion of circularly permuted human Interleukin-2 and Interleukin-2 Receptor alpha
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ALS BEAMLINE 4.2.2 |
Synchrotron site | ALS |
Beamline | 4.2.2 |
Temperature [K] | 100 |
Detector technology | CMOS |
Collection date | 2015-08-12 |
Detector | RDI CMOS_8M |
Wavelength(s) | 1.0 |
Spacegroup name | P 32 2 1 |
Unit cell lengths | 86.809, 86.809, 119.576 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 63.645 - 3.400 |
R-factor | 0.2768 |
Rwork | 0.275 |
R-free | 0.29730 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1z92 |
RMSD bond length | 0.002 |
RMSD bond angle | 0.654 |
Data reduction software | XDS |
Data scaling software | Aimless |
Phasing software | MOLREP |
Refinement software | PHENIX (dev_1951) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 63.645 | 3.522 |
High resolution limit [Å] | 3.400 | 3.400 |
Rmerge | 0.185 | 0.185 |
Number of reflections | 7538 | 750 |
<I/σ(I)> | 12.8 | |
Completeness [%] | 100.0 | 100 |
Redundancy | 10.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 293 | An equal volume of protein was mixed with crystallization buffer, 25 % (w/v) PEG 3350, 0.2 M MgCl2, 0.1 M Hepes 7.5. Large crystals appeared within 48-72 hours, and were frozen in a cryoprotectant consisting of mother liquor with 10 % glycerol |