6LP5
Structure of Sinonovacula constricta ferritin
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SSRF BEAMLINE BL19U1 |
| Synchrotron site | SSRF |
| Beamline | BL19U1 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2018-07-04 |
| Detector | DECTRIS PILATUS 2M |
| Wavelength(s) | 0.97892 |
| Spacegroup name | I 4 |
| Unit cell lengths | 154.510, 154.510, 129.500 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 109.260 - 1.980 |
| R-factor | 0.1654 |
| Rwork | 0.163 |
| R-free | 0.20250 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1bg7 |
| RMSD bond length | 0.026 |
| RMSD bond angle | 2.184 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | BALBES |
| Refinement software | REFMAC (5.8.0135) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 109.260 | 2.010 |
| High resolution limit [Å] | 1.980 | 1.980 |
| Number of reflections | 697312 | 104802 |
| <I/σ(I)> | 38.5 | |
| Completeness [%] | 99.3 | |
| Redundancy | 6.7 | |
| CC(1/2) | 0.980 | 0.980 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 291.15 | 1 uL of protein (10 mg/mL, 25 mM Tris-HCl, 150 mM NaCl, pH 8.0), 1 uL precipitant solution (1.0 M 1,6-hexanediol, 0.01 M cobalt (2+) chloride hexahydrate, 0.1 M sodium acetate trihydrate pH 4.6) |






