6EQV
X-ray structure of the proprotein convertase furin bound with the competitive inhibitor Phac-Cit-Val-Arg-Amba
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | BESSY BEAMLINE 14.1 |
Synchrotron site | BESSY |
Beamline | 14.1 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2014-11-24 |
Detector | DECTRIS PILATUS 6M |
Wavelength(s) | 0.918409 |
Spacegroup name | P 65 2 2 |
Unit cell lengths | 131.601, 131.601, 155.638 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 45.976 - 1.895 |
R-factor | 0.1646 |
Rwork | 0.164 |
R-free | 0.18210 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 5jxh |
RMSD bond length | 0.006 |
RMSD bond angle | 0.830 |
Data reduction software | XDS |
Data scaling software | XDS |
Phasing software | PHENIX |
Refinement software | PHENIX ((1.11.1_2575: ???)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 47.200 | 2.010 |
High resolution limit [Å] | 1.890 | 1.890 |
Rmerge | 0.109 | 0.723 |
Rmeas | 0.118 | 0.786 |
Number of reflections | 63141 | 9981 |
<I/σ(I)> | 14.97 | 2.84 |
Completeness [%] | 99.4 | |
Redundancy | 6.54 | |
CC(1/2) | 0.998 | 0.844 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 293.15 | CRYSTALLIZATION SOLUTION: 100mM MES, 200mM K/NaH2PO4, PH 5.5-6.0, 3-4M NaCl, 3% DMSO; RESERVOIR SOLUTION: 3-4 M NaCl |