4AVS
Structure of N-Acetyl-L-Proline bound to Serum Amyloid P Component
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 |
| Detector | ADSC QUANTUM 4 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 94.966, 69.937, 102.347 |
| Unit cell angles | 90.00, 96.97, 90.00 |
Refinement procedure
| Resolution | 30.479 - 1.399 |
| R-factor | 0.1443 |
| Rwork | 0.144 |
| R-free | 0.17030 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1sac |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.365 |
| 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] | 30.430 | 1.480 |
| High resolution limit [Å] | 1.400 | 1.400 |
| Rmerge | 0.130 | 0.430 |
| Number of reflections | 251592 | |
| <I/σ(I)> | 7.2 | 3.5 |
| Completeness [%] | 96.4 | 95.7 |
| Redundancy | 3.6 | 3.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 8 | 0.06 M TRIS-HCL, PH 8, 16% PEG 550 MME, 0.01 M CACL2, 0.08 M NACL AND 0.1% NAN3 |
