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 |