7CNQ
Crystal structure of Agrobacterium tumefaciens aconitase X (holo-form)
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SPRING-8 BEAMLINE BL41XU |
Synchrotron site | SPring-8 |
Beamline | BL41XU |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2018-07-18 |
Detector | DECTRIS EIGER X 16M |
Wavelength(s) | 1.0 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 73.250, 73.446, 175.184 |
Unit cell angles | 90.00, 94.13, 90.00 |
Refinement procedure
Resolution | 48.984 - 2.000 |
R-factor | 0.211 |
Rwork | 0.209 |
R-free | 0.25310 |
Structure solution method | MOLECULAR REPLACEMENT |
Data scaling software | XDS |
Phasing software | PHASER |
Refinement software | PHENIX (1.14_3260) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 48.984 | 48.984 | 2.120 |
High resolution limit [Å] | 2.000 | 5.950 | 2.000 |
Rmerge | 0.136 | 0.040 | 0.899 |
Rmeas | 0.160 | 0.046 | 1.054 |
Number of reflections | 242653 | 9300 | 38641 |
<I/σ(I)> | 5.51 | 15.11 | 1.26 |
Completeness [%] | 98.1 | 99.2 | 96.6 |
Redundancy | 3.546 | 3.758 | 3.661 |
CC(1/2) | 0.997 | 0.999 | 0.721 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 293 | PEG 3350, Bis-Tris |