6XNL
GCN4-p1 Peptide Trimer with iodo-phenylalanine residue at position 16 (IPF-F16)
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ALS BEAMLINE 4.2.2 |
Synchrotron site | ALS |
Beamline | 4.2.2 |
Temperature [K] | 100 |
Detector technology | CMOS |
Collection date | 2018-01-09 |
Detector | RDI CMOS_8M |
Wavelength(s) | 0.83 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 59.069, 34.848, 46.712 |
Unit cell angles | 90.00, 100.44, 90.00 |
Refinement procedure
Resolution | 19.850 - 2.200 |
R-factor | 0.2322 |
Rwork | 0.222 |
R-free | 0.32110 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1swi |
RMSD bond length | 0.008 |
RMSD bond angle | 1.146 |
Data reduction software | HKL-2000 |
Data scaling software | Aimless |
Phasing software | PHENIX |
Refinement software | PHENIX (1.16_3549) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 19.850 | 2.280 |
High resolution limit [Å] | 2.200 | 2.200 |
Rmerge | 0.071 | 0.429 |
Rmeas | 0.100 | 0.607 |
Rpim | 0.071 | 0.429 |
Number of reflections | 8716 | 695 |
<I/σ(I)> | 14.32 | 2.67 |
Completeness [%] | 97.9 | |
Redundancy | 1.8 | |
CC(1/2) | 0.986 | 0.462 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7 | 298 | Crystallization drops were prepared by mixing 2 uL of stock peptide solution with 2 uL of mother liquor and allowed to equilibrate at 298 K over a well containing 500 uL of mother liquor. The stock peptide solution (total concentration 1.5 mM) was prepared by mixing 2:1 ratios of the A16 peptide with IPF-F16 in 10 mM potassium phosphate, 100 mM potassium chloride pH 7.0. |