7FCS
Crystal structure of the N-terminal domain of mutants of Human Apolipoprotein-E (ApoE)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | RRCAT INDUS-2 BEAMLINE PX-BL21 |
| Synchrotron site | RRCAT INDUS-2 |
| Beamline | PX-BL21 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2021-02-15 |
| Detector | RAYONIX MX-225 |
| Wavelength(s) | 0.97949 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 40.870, 53.493, 85.776 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 25.890 - 1.600 |
| R-factor | 0.1896 |
| Rwork | 0.188 |
| R-free | 0.21580 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1gs9 |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.034 |
| Data reduction software | XDS |
| Data scaling software | Aimless (0.7.4) |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.19) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 45.390 | 45.390 | 1.630 |
| High resolution limit [Å] | 1.600 | 8.760 | 1.600 |
| Rmerge | 0.036 | 0.035 | 0.699 |
| Rmeas | 0.040 | 0.042 | 0.784 |
| Rpim | 0.018 | 0.022 | 0.349 |
| Total number of observations | 120391 | 687 | 6045 |
| Number of reflections | 25447 | 183 | 1261 |
| <I/σ(I)> | 20.4 | 44.9 | 2.1 |
| Completeness [%] | 99.6 | 94.3 | 100 |
| Redundancy | 4.7 | 3.8 | 4.8 |
| CC(1/2) | 0.999 | 0.995 | 0.731 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | MICROBATCH | 5.15 | 294 | 100 mM sodium cacodylate, 28% PEG 400 |
