4AOC
crystal structure of BC2L-A Lectin from Burkolderia cenocepacia in complex with methyl-heptoside
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID23-2 |
Synchrotron site | ESRF |
Beamline | ID23-2 |
Temperature [K] | 100 |
Detector technology | CCD |
Detector | MARMOSAIC 225 mm CCD |
Spacegroup name | C 2 2 21 |
Unit cell lengths | 50.000, 185.140, 186.210 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 93.110 - 2.700 |
R-factor | 0.19545 |
Rwork | 0.192 |
R-free | 0.25320 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2wr9 |
RMSD bond length | 0.011 |
RMSD bond angle | 1.569 |
Data reduction software | XDS |
Data scaling software | SCALA |
Phasing software | MOLREP |
Refinement software | REFMAC (5.6.0117) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 48.270 | 2.850 |
High resolution limit [Å] | 2.700 | 2.700 |
Rmerge | 0.140 | 0.520 |
Number of reflections | 24256 | |
<I/σ(I)> | 10.2 | 2.9 |
Completeness [%] | 99.6 | 81.7 |
Redundancy | 4.8 | 4.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 |