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 |