2RIO
Structure of the dual enzyme Ire1 reveals the basis for catalysis and regulation of non-conventional splicing
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 19-BM |
Synchrotron site | APS |
Beamline | 19-BM |
Collection date | 2006-03-24 |
Wavelength(s) | 0.97883 |
Spacegroup name | P 65 |
Unit cell lengths | 130.307, 130.307, 175.011 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 19.830 - 2.400 |
R-factor | 0.22443 |
Rwork | 0.222 |
R-free | 0.26637 |
Structure solution method | SAD |
RMSD bond length | 0.029 |
RMSD bond angle | 2.495 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | SHELXS |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 3.110 |
High resolution limit [Å] | 2.400 | 2.400 |
Number of reflections | 66131 | |
<I/σ(I)> | 7.2 | 8.1 |
Completeness [%] | 100.0 | 100 |
Redundancy | 43.4 | 6.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8 | 294 | 50mM Tris-Cl (pH 8.0), 200mM KOAc, 50mM SrOAc, 10mM MgCl2 and 10% PEG 8K , VAPOR DIFFUSION, HANGING DROP, temperature 294K |