5FRQ
Crystal Structure of Helicobacter pylori beta clamp bound to DNA ligase peptide
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE BM14 |
Synchrotron site | ESRF |
Beamline | BM14 |
Temperature [K] | 289 |
Detector technology | CCD |
Collection date | 2015-11-20 |
Detector | MARRESEARCH |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 64.829, 146.147, 179.075 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 113.230 - 2.900 |
R-factor | 0.23302 |
Rwork | 0.231 |
R-free | 0.26154 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4rki |
RMSD bond length | 0.013 |
RMSD bond angle | 1.807 |
Refinement software | REFMAC (5.8.0135) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 50.000 |
High resolution limit [Å] | 2.900 | 2.900 |
Rmerge | 0.100 | 0.520 |
Number of reflections | 35997 | |
<I/σ(I)> | 11 | 1.9 |
Completeness [%] | 94.3 | 95 |
Redundancy | 4.2 | 4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 6% W/V PEG 20,000, 20% V/V PEG MME550, 0.01M MGCL2, 0.1M MOPS/HEPES-NA PH7.3, 0.2M AMMONIUM CITRATE |