2WYP
Crystal structure of sialic acid binding protein
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-4 |
| Synchrotron site | ESRF |
| Beamline | ID14-4 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2009-07-27 |
| Detector | ADSC CCD |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 47.836, 74.489, 88.151 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 28.450 - 1.500 |
| R-factor | 0.139 |
| Rwork | 0.136 |
| R-free | 0.19500 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2v4c |
| RMSD bond length | 0.017 |
| RMSD bond angle | 1.629 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | REFMAC |
| Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.520 |
| High resolution limit [Å] | 1.490 | 1.490 |
| Rmerge | 0.110 | 0.400 |
| Number of reflections | 46426 | |
| <I/σ(I)> | 11.8 | 3.8 |
| Completeness [%] | 90.1 | 99.2 |
| Redundancy | 6.2 | 5.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 7 | 277 | 30 MG/ML SIAP (IN 20 MM HEPES, 10 MM NACL AND KDN, PH 8.0) AND EQUAL VOLUME OF RESERVOIR SOLUTION (100MM MES PH 6.0, 28.5% PEG 6K, 200MM SODIUM THIOCYANATE), TEMPERATURE 277K |
