6EC0
Crystal structure of the wild-type heterocomplex between coil 1B domains of human intermediate filament proteins keratin 1 (KRT1) and keratin 10 (KRT10)
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 24-ID-C |
Synchrotron site | APS |
Beamline | 24-ID-C |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2017-07-06 |
Detector | DECTRIS PILATUS 6M-F |
Wavelength(s) | 0.9795 |
Spacegroup name | P 31 2 1 |
Unit cell lengths | 106.685, 106.685, 70.321 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 46.196 - 2.983 |
R-factor | 0.2822 |
Rwork | 0.281 |
R-free | 0.30010 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | Phase problem initially solved using SAD on an isomorphous crystal whose data was collected at the cadmium edge (8500eV). This structure was used as starting model in MolRep to obtain the higher resolution KRT1/KRT10 1B structure. |
RMSD bond length | 0.006 |
RMSD bond angle | 0.896 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | MOLREP |
Refinement software | PHENIX |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 50.000 | 50.000 | 3.050 |
High resolution limit [Å] | 2.983 | 8.130 | 2.983 |
Rmerge | 0.132 | 0.050 | 1.185 |
Rmeas | 0.141 | 0.053 | 1.285 |
Rpim | 0.047 | 0.017 | 0.477 |
Number of reflections | 8681 | 536 | 206 |
<I/σ(I)> | 4.3 | ||
Completeness [%] | 89.6 | 100 | 42.7 |
Redundancy | 8 | 8.8 | 5 |
CC(1/2) | 0.999 | 0.640 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 298 | 11% PEG 3350, 0.1 M HEPES, 5 mM cobalt chloride, 5 mM cadmium chloride, 5 mM magnesium chloride, 5 mM nickel chloride |