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 |
