6VZD
N-terminal domain of mouse surfactant protein B (K46E/R51E mutant) with bound lipid
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 24-ID-E |
| Synchrotron site | APS |
| Beamline | 24-ID-E |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2019-12-10 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 0.979 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 49.793, 66.124, 59.620 |
| Unit cell angles | 90.00, 97.37, 90.00 |
Refinement procedure
| Resolution | 59.130 - 1.880 |
| R-factor | 0.1727 |
| Rwork | 0.170 |
| R-free | 0.21750 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 6VYN (lipid removed) |
| RMSD bond length | 0.006 |
| RMSD bond angle | 0.736 |
| Data reduction software | XDS |
| Data scaling software | XDS |
| Phasing software | PHENIX |
| Refinement software | PHENIX (1.17.1_3660) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 59.130 | 1.947 |
| High resolution limit [Å] | 1.880 | 1.880 |
| Rmerge | 0.100 | 1.511 |
| Number of reflections | 31237 | 2186 |
| <I/σ(I)> | 40.86 | 2.41 |
| Completeness [%] | 92.2 | |
| Redundancy | 53.8 | |
| CC(1/2) | 1.000 | 0.897 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5.4 | 293.15 | 100 mM citrate buffer pH 5.4, 23-25% PEG 4000, 14-15% 2-propanol |






