7BFY
Structure of the apo form of the N terminal domain of Bc2L-C lectin (1-131)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SOLEIL BEAMLINE PROXIMA 1 |
| Synchrotron site | SOLEIL |
| Beamline | PROXIMA 1 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2020-09-04 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 0.9801 |
| Spacegroup name | P 63 |
| Unit cell lengths | 42.987, 42.987, 94.678 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 19.970 - 1.500 |
| R-factor | 0.1502 |
| Rwork | 0.149 |
| R-free | 0.17780 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 6tig |
| RMSD bond length | 0.014 |
| RMSD bond angle | 1.851 |
| Data reduction software | XDS |
| Data scaling software | Aimless (0.7.4) |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0267) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 19.970 | 19.970 | 1.530 |
| High resolution limit [Å] | 1.500 | 8.220 | 1.500 |
| Rmerge | 0.083 | 0.062 | 0.454 |
| Rmeas | 0.085 | 0.065 | 0.471 |
| Rpim | 0.021 | 0.020 | 0.123 |
| Total number of observations | 261006 | 1325 | 12693 |
| Number of reflections | 15915 | 97 | 820 |
| <I/σ(I)> | 21.7 | 36.2 | 5.9 |
| Completeness [%] | 99.9 | 91.5 | 100 |
| Redundancy | 16.4 | 13.7 | 15.5 |
| CC(1/2) | 0.999 | 0.988 | 0.935 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7 | 292 | 5.5 mg/ml of protein, 1.2 M sodium citrate, at 292 K temperature and cryoprotected with 2.5 M sodium malonate |
