3UC4
The crystal structure of Snf1-related kinase 2.6
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 21-ID-D |
Synchrotron site | APS |
Beamline | 21-ID-D |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2010-10-16 |
Detector | MARRESEARCH |
Wavelength(s) | 1.0 |
Spacegroup name | C 2 2 21 |
Unit cell lengths | 76.111, 171.536, 116.242 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 29.850 - 2.300 |
R-factor | 0.2225 |
Rwork | 0.221 |
R-free | 0.24610 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.012 |
RMSD bond angle | 1.174 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | PHASER (1.3.2) |
Refinement software | REFMAC (5.5.0072) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 2.380 |
High resolution limit [Å] | 2.300 | 2.300 |
Number of reflections | 34149 | |
Completeness [%] | 91.0 | 100 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION | 7.5 | 298 | PEG 3350, ammonium sulfate, pH 7.5, VAPOR DIFFUSION, temperature 298K |