6K6T
Crystal structure of a standalone versatile EAL protein from Vibrio cholerae O395 - c-di-IMP bound form
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SEALED TUBE |
Source details | BRUKER IMUS MICROFOCUS |
Temperature [K] | 273 |
Detector technology | IMAGE PLATE |
Collection date | 2018-05-04 |
Detector | MAR scanner 345 mm plate |
Wavelength(s) | 1.54 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 73.450, 42.540, 155.040 |
Unit cell angles | 90.00, 94.65, 90.00 |
Refinement procedure
Resolution | 51.114 - 2.200 |
R-factor | 0.1994 |
Rwork | 0.197 |
R-free | 0.25190 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3gfx |
RMSD bond length | 0.015 |
RMSD bond angle | 1.285 |
Data reduction software | iMOSFLM |
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] | 51.510 | 51.510 | 2.270 |
High resolution limit [Å] | 2.200 | 9.070 | 2.200 |
Rmerge | 0.161 | 0.102 | 0.647 |
Rmeas | 0.194 | 0.125 | 0.777 |
Rpim | 0.107 | 0.070 | 0.426 |
Total number of observations | 148871 | 2180 | 12648 |
Number of reflections | 47970 | 742 | 4064 |
<I/σ(I)> | 4.1 | 7.1 | 1.6 |
Completeness [%] | 97.8 | 96.3 | 96.1 |
Redundancy | 3.1 | 2.9 | 3.1 |
CC(1/2) | 0.982 | 0.982 | 0.680 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 5.6 | 293 | 0.2M Ammonium acetate, 0.1M Sodium citrate tribasic dihydrate pH 5.6, 30% w/v Polyethylene glycol 4000 |