6IH7
Crystal structure of a standalone versatile EAL protein from Vibrio cholerae O395 - 3',3'-cGAMP bound form
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SEALED TUBE |
Source details | BRUKER IMUS MICROFOCUS |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2018-02-08 |
Detector | MAR scanner 345 mm plate |
Wavelength(s) | 1.54179 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 157.899, 42.600, 73.330 |
Unit cell angles | 90.00, 94.91, 90.00 |
Refinement procedure
Resolution | 55.974 - 2.250 |
R-factor | 0.1842 |
Rwork | 0.181 |
R-free | 0.23970 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3gfx |
RMSD bond length | 0.010 |
RMSD bond angle | 0.972 |
Data reduction software | MOSFLM |
Data scaling software | Aimless (0.3.11) |
Phasing software | PHENIX |
Refinement software | PHENIX (1.12_2829) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 55.974 | 55.970 | 2.320 |
High resolution limit [Å] | 2.250 | 9.000 | 2.250 |
Rmerge | 0.042 | 0.037 | 0.169 |
Rmeas | 0.051 | 0.045 | 0.205 |
Rpim | 0.028 | 0.025 | 0.115 |
Number of reflections | 22200 | 378 | 1951 |
<I/σ(I)> | 15.1 | ||
Completeness [%] | 95.1 | 92.6 | 93.3 |
Redundancy | 3.2 | 3 | 3.2 |
CC(1/2) | 0.998 | 0.995 | 0.976 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 293 | PEG4000, sodium acetate, tris |