8SQQ
Crystal Structure of Bacterioferritin (Bfr) from Brucella abortus (Apo Cubic Form 2, F16L mutant)
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | NSLS-II BEAMLINE 19-ID |
Synchrotron site | NSLS-II |
Beamline | 19-ID |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2022-03-14 |
Detector | DECTRIS EIGER2 XE 9M |
Wavelength(s) | 0.9795 |
Spacegroup name | F 4 3 2 |
Unit cell lengths | 171.516, 171.516, 171.516 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 39.350 - 2.250 |
R-factor | 0.1917 |
Rwork | 0.189 |
R-free | 0.24550 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.013 |
RMSD bond angle | 1.139 |
Data reduction software | XDS |
Data scaling software | Aimless |
Phasing software | PHASER |
Refinement software | PHENIX ((1.21rc1_4933: ???)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 42.880 | 2.320 |
High resolution limit [Å] | 2.250 | 2.250 |
Rmerge | 0.206 | 2.857 |
Rmeas | 0.209 | 2.892 |
Rpim | 0.033 | 0.448 |
Total number of observations | 419133 | 39593 |
Number of reflections | 10780 | 961 |
<I/σ(I)> | 18.1 | 1.9 |
Completeness [%] | 100.0 | |
Redundancy | 38.9 | 41.2 |
CC(1/2) | 0.999 | 0.668 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 4.5 | 291 | Berkeley G7: 1.5M ammonium sulfate, 5% (v/v) MPD, 100 mM sodium acetate pH 4.5, BrabA.00028.a.A1.PW39164 at 10 mg/mL. Plate: 10390, well G7 drop 2. Puck: PSL-1810, Cryo: 2.5M lithium sulfate |