2VLO
K97A mutant of E9 DNase domain in complex with Im9
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID14-3 |
Synchrotron site | ESRF |
Beamline | ID14-3 |
Temperature [K] | 110 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 36.382, 78.618, 40.217 |
Unit cell angles | 90.00, 99.36, 90.00 |
Refinement procedure
Resolution | 27.950 - 1.800 |
R-factor | 0.177 |
Rwork | 0.174 |
R-free | 0.22800 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1emv |
RMSD bond length | 0.019 |
RMSD bond angle | 1.811 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | MOLREP |
Refinement software | REFMAC (5.2.0001) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 1.900 |
High resolution limit [Å] | 1.800 | 1.800 |
Rmerge | 0.060 | 0.250 |
Number of reflections | 19052 | |
<I/σ(I)> | 13.9 | 3.9 |
Completeness [%] | 91.9 | 91.9 |
Redundancy | 2.8 | 1.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 |