4OZ6
Structure of the Branched Intermediate in Protein Splicing
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 24-ID-E |
Synchrotron site | APS |
Beamline | 24-ID-E |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2011-03-25 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 0.97923 |
Spacegroup name | P 41 21 2 |
Unit cell lengths | 58.746, 58.746, 111.762 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 40.489 - 2.786 |
R-factor | 0.2314 |
Rwork | 0.230 |
R-free | 0.26170 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1am2 |
RMSD bond length | 0.003 |
RMSD bond angle | 0.770 |
Data scaling software | HKL-2000 |
Phasing software | PHASER |
Refinement software | PHENIX ((phenix.refine: 1.7_650)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.880 |
High resolution limit [Å] | 2.780 | 2.780 |
Number of reflections | 5310 | |
<I/σ(I)> | 39.6 | 9.7 |
Completeness [%] | 99.7 | 96.4 |
Redundancy | 8.7 | 7.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 277 | Crystals were obtained by mixing 1 ul of protein with 1 ul of crystallization solution (100mM sodium cacodylate, pH 6.5, 200mM magnesium acetate, and 20% (w/v) PEG 8000. |