2OK2
MutS C-terminal domain fused to Maltose Binding Protein
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SSRL BEAMLINE BL11-1 |
Synchrotron site | SSRL |
Beamline | BL11-1 |
Temperature [K] | 200 |
Detector technology | CCD |
Collection date | 2006-07-15 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 0.9795 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 174.289, 88.361, 61.353 |
Unit cell angles | 90.00, 106.80, 90.00 |
Refinement procedure
Resolution | 20.000 - 2.000 |
R-factor | 0.20501 |
Rwork | 0.201 |
R-free | 0.27725 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1fqc |
RMSD bond length | 0.023 |
RMSD bond angle | 1.914 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 2.070 |
High resolution limit [Å] | 2.000 | 2.000 |
Number of reflections | 59119 | |
<I/σ(I)> | 47 | 3.2 |
Completeness [%] | 97.9 | 95.6 |
Redundancy | 4 | 3.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 5.6 | 298 | 15% PEG 4K, 100 mM sodium citrate, 100 mM lithium acetate, pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 298K |