7KNF
1.80A resolution structure of independent Phosphoglycerate mutase from C. elegans in complex with a macrocyclic peptide inhibitor (Ce-1 NHOH)
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 17-ID |
Synchrotron site | APS |
Beamline | 17-ID |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2019-02-16 |
Detector | DECTRIS PILATUS 6M |
Wavelength(s) | 1.00000 |
Spacegroup name | P 1 2 1 |
Unit cell lengths | 73.669, 75.846, 100.424 |
Unit cell angles | 90.00, 98.31, 90.00 |
Refinement procedure
Resolution | 44.130 - 1.800 |
R-factor | 0.1542 |
Rwork | 0.152 |
R-free | 0.19430 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 5kgn |
Data reduction software | XDS |
Data scaling software | Aimless (0.7.4) |
Phasing software | PHASER |
Refinement software | PHENIX (1.18rc1_3769) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 48.600 | 48.600 | 1.830 |
High resolution limit [Å] | 1.800 | 9.860 | 1.800 |
Rmerge | 0.130 | 0.047 | 1.217 |
Total number of observations | 767614 | 4923 | 36958 |
Number of reflections | 101405 | 661 | 4911 |
<I/σ(I)> | 11.2 | 35.3 | 1.8 |
Completeness [%] | 100.0 | 98.9 | 99.8 |
Redundancy | 7.6 | 7.4 | 7.5 |
CC(1/2) | 0.998 | 0.998 | 0.735 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 293 | 25% (w/v) PEG 3350, 0.1 M Bis-Tris |