2W08
The structure of serum amyloid P component bound to 0-phospho- threonine
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-2 |
| Synchrotron site | ESRF |
| Beamline | ID14-2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2004-07-15 |
| Detector | MARRESEARCH |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 94.769, 69.435, 102.063 |
| Unit cell angles | 90.00, 97.05, 90.00 |
Refinement procedure
| Resolution | 47.480 - 1.700 |
| R-factor | 0.154 |
| Rwork | 0.154 |
| R-free | 0.17600 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1sac |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.192 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | MOLREP |
| Refinement software | PHENIX ((PHENIX.REFINE)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 47.670 | 1.780 |
| High resolution limit [Å] | 1.700 | 1.700 |
| Rmerge | 0.110 | 0.380 |
| Number of reflections | 140019 | |
| <I/σ(I)> | 16.7 | 9.3 |
| Completeness [%] | 97.0 | 95.6 |
| Redundancy | 5.6 | 4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 8 | 0.06M TRIS-HCL PH8, 16% PEG 550MME, 0.01M CACL2, 0.08M NACL, 0.1% NAN3, 14.2MG/ML PROTEIN, 50MM LIGAND |
