4A5K
Structural analyses of Slm1-PH domain demonstrate ligand binding in the non-canonical site
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID23-1 |
Synchrotron site | ESRF |
Beamline | ID23-1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2011-01-27 |
Detector | ADSC QUANTUM 315r |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 37.300, 82.300, 76.400 |
Unit cell angles | 90.00, 90.10, 90.00 |
Refinement procedure
Resolution | 38.200 - 1.760 |
R-factor | 0.1893 |
Rwork | 0.188 |
R-free | 0.22700 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3nsu |
RMSD bond length | 0.006 |
RMSD bond angle | 1.031 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | PHASER |
Refinement software | PHENIX ((PHENIX.REFINE: 1.5_2)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 1.700 |
High resolution limit [Å] | 1.600 | 1.600 |
Rmerge | 0.050 | 0.700 |
Number of reflections | 49444 | |
<I/σ(I)> | 23 | 2.2 |
Completeness [%] | 83.0 | 40 |
Redundancy | 6.1 | 3.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 7 | pH 7.0 |