6PXZ
Crystal Structure of mouse Serum Amyloid A3 (SAA3) in the trimeric form
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 23-ID-D |
| Synchrotron site | APS |
| Beamline | 23-ID-D |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2015-12-11 |
| Detector | DECTRIS PILATUS 6M |
| Wavelength(s) | 1.0 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 52.317, 74.882, 89.940 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 28.840 - 1.700 |
| R-factor | 0.219 |
| Rwork | 0.217 |
| R-free | 0.25190 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4q5g |
| RMSD bond length | 0.007 |
| RMSD bond angle | 0.893 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-3000 |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.8_1069) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 1.730 |
| High resolution limit [Å] | 1.700 | 4.610 | 1.700 |
| Rmerge | 0.071 | 0.036 | 1.461 |
| Rmeas | 0.075 | 0.039 | 1.561 |
| Rpim | 0.026 | 0.014 | 0.544 |
| Total number of observations | 333363 | ||
| Number of reflections | 39758 | 2145 | 1945 |
| <I/σ(I)> | 7.7 | ||
| Completeness [%] | 99.9 | 98.8 | 100 |
| Redundancy | 8.4 | 7.8 | 8.1 |
| CC(1/2) | 0.998 | 0.569 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 291 | 0.2 M trisodium citrate, 0.1 M HEPES, pH 7.5, 6% PEG6000, 10% isopropanol |
