7L33
X-ray Structure of a Cu-Bound De Novo Designed Peptide Trimer
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 21-ID-G |
Synchrotron site | APS |
Beamline | 21-ID-G |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2020-06-27 |
Detector | MARMOSAIC 300 mm CCD |
Wavelength(s) | 0.97856 |
Spacegroup name | P 63 |
Unit cell lengths | 39.260, 39.260, 83.630 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 20.907 - 1.450 |
R-factor | 0.2698 |
Rwork | 0.269 |
R-free | 0.29450 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4dzl |
Data reduction software | XDS |
Data scaling software | Aimless (0.7.4) |
Phasing software | PHASER |
Refinement software | PHENIX (1.14_3260) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 31.500 | 31.500 | 1.490 |
High resolution limit [Å] | 1.450 | 6.480 | 1.450 |
Rmerge | 0.097 | 0.074 | 3.791 |
Rmeas | 0.102 | 0.078 | 4.074 |
Rpim | 0.031 | 0.025 | 1.439 |
Total number of observations | 138001 | 1546 | 6128 |
Number of reflections | 12815 | 154 | 853 |
<I/σ(I)> | 10.2 | 30 | 0.6 |
Completeness [%] | 98.9 | 98 | 90.8 |
Redundancy | 10.8 | 10 | 7.2 |
CC(1/2) | 0.998 | 0.999 | 0.372 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 298 | 0.1 M Tris pH 8.5, 0.2 M MgCl2.6H20, 30% PEG 4000 |