7LUR
Stable Effector Functionless 2 (SEFL2) IgG1 Fc Scaffold Bound to a Minimized Version of the B-domain (Mini-Z) from Protein A Called Z34C
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ALS BEAMLINE 5.0.2 |
| Synchrotron site | ALS |
| Beamline | 5.0.2 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2017-03-17 |
| Detector | PSI PILATUS 6M |
| Wavelength(s) | 1.0 |
| Spacegroup name | I 1 2 1 |
| Unit cell lengths | 63.438, 69.335, 135.421 |
| Unit cell angles | 90.00, 98.64, 90.00 |
Refinement procedure
| Resolution | 40.360 - 1.950 |
| R-factor | 0.218 |
| Rwork | 0.216 |
| R-free | 0.26020 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1l6x |
| Data reduction software | XDS |
| Data scaling software | Aimless (0.5.32) |
| Phasing software | MOLREP |
| Refinement software | PHENIX (1.18.2_3874) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 46.510 | 46.510 | 2.000 |
| High resolution limit [Å] | 1.950 | 8.940 | 1.950 |
| Rmerge | 0.246 | 0.080 | 1.897 |
| Total number of observations | 283884 | 3065 | 20377 |
| Number of reflections | 42098 | 467 | 2932 |
| <I/σ(I)> | 6.9 | 22.7 | 1.3 |
| Completeness [%] | 99.3 | 98.8 | 98.5 |
| Redundancy | 6.7 | 6.6 | 6.9 |
| CC(1/2) | 0.991 | 0.991 | 0.478 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | EVAPORATION | 293 | 0.2 M ammonium tartrate, 20% (w/v) PEG 3350, 10% NDSB-221 |
