3MN3
An inhibited conformation for the protein kinase domain of the Saccharomyces cerevisiae AMPK homolog Snf1
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | NSLS BEAMLINE X4C |
Synchrotron site | NSLS |
Beamline | X4C |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2009-04-01 |
Detector | MAR scanner 345 mm plate |
Wavelength(s) | 0.9815 |
Spacegroup name | I 41 2 2 |
Unit cell lengths | 76.981, 76.981, 286.215 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 30.000 - 2.380 |
R-factor | 0.231 |
Rwork | 0.230 |
R-free | 0.24600 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.010 |
RMSD bond angle | 1.270 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | COMO |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 2.480 |
High resolution limit [Å] | 2.380 | 2.380 |
Number of reflections | 19799 | |
Completeness [%] | 99.0 | 99 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION | 7.5 | 294 | 10% (w/v) PEG3350 and 50mM Na2SO4, pH 7.5, VAPOR DIFFUSION, temperature 294K |