2XA5
Structure of substrate binding protein SiaP (A11N) in complex with Neu5Ac
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 QUANTUM 210 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 47.818, 74.700, 87.254 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 32.229 - 1.090 |
| R-factor | 0.11895 |
| Rwork | 0.118 |
| R-free | 0.14436 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2v4c |
| RMSD bond length | 0.022 |
| RMSD bond angle | 1.933 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALEPACK |
| Phasing software | REFMAC |
| Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 74.000 | 1.150 |
| High resolution limit [Å] | 1.090 | 1.090 |
| Rmerge | 0.060 | 0.340 |
| Number of reflections | 128703 | |
| <I/σ(I)> | 13.2 | 3.8 |
| Completeness [%] | 99.4 | 98.9 |
| Redundancy | 5.5 | 5.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 7 | 277 | 30 MG/ML SIAP (IN 20 MM HEPES, 10 MM NACL AND NEU5AC, PH 8.0) AND RESERVOIR SOLUTION (100MM MES PH 6.0, 28.5% PEG 6K, 50MM SODIUM FLUORIDE); 2:1 RATIO RESPECTIVELY; TEMPERATURE 277K |
