4H3T
Crystal structure of CRISPR-associated protein Cse1 from Acidimicrobium ferrooxidans
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 19-ID |
Synchrotron site | APS |
Beamline | 19-ID |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2011-08-03 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 0.97915 |
Spacegroup name | I 41 2 2 |
Unit cell lengths | 137.017, 137.017, 203.537 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 29.720 - 2.030 |
R-factor | 0.182 |
Rwork | 0.182 |
R-free | 0.19910 |
Structure solution method | SAD |
RMSD bond length | 0.014 |
RMSD bond angle | 1.110 |
Data reduction software | HKL-3000 |
Data scaling software | HKL-3000 |
Phasing software | MLPHARE |
Refinement software | BUSTER (2.10.0) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.070 |
High resolution limit [Å] | 2.030 | 2.030 |
Rmerge | 0.070 | 0.730 |
Number of reflections | 62132 | |
<I/σ(I)> | 25.3 | 2.4 |
Completeness [%] | 99.0 | 99.9 |
Redundancy | 12 | 9.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 289 | 0.2 M proline, 0.1 M HEPES/NaOH, 10% PEG3350, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 289K |