Bromine in PDB 7vso: Serial Femtosecond Crystallography (Sfx) of Ground State Bacteriorhodopsin Crystallized From Bicelles in Complex with HAD16 Determined Using 7-Kev X-Ray Free Electron Laser (Xfel) at Sacla

The structure of Serial Femtosecond Crystallography (Sfx) of Ground State Bacteriorhodopsin Crystallized From Bicelles in Complex with HAD16 Determined Using 7-Kev X-Ray Free Electron Laser (Xfel) at Sacla, PDB code: 7vso was solved by E.Mizohata, T.Nakane, S.Hanashima, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	42.90 / 2.35
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	46.2, 103, 128.7, 90, 90, 90
R / Rfree (%)	15.8 / 21

The structure of Serial Femtosecond Crystallography (Sfx) of Ground State Bacteriorhodopsin Crystallized From Bicelles in Complex with HAD16 Determined Using 7-Kev X-Ray Free Electron Laser (Xfel) at Sacla also contains other interesting chemical elements:

Iodine

(I)

3 atoms

The binding sites of Bromine atom in the Serial Femtosecond Crystallography (Sfx) of Ground State Bacteriorhodopsin Crystallized From Bicelles in Complex with HAD16 Determined Using 7-Kev X-Ray Free Electron Laser (Xfel) at Sacla (pdb code 7vso). This binding sites where shown within 5.0 Angstroms radius around Bromine atom.
In total 2 binding sites of Bromine where determined in the Serial Femtosecond Crystallography (Sfx) of Ground State Bacteriorhodopsin Crystallized From Bicelles in Complex with HAD16 Determined Using 7-Kev X-Ray Free Electron Laser (Xfel) at Sacla, PDB code: 7vso:
Jump to Bromine binding site number: 1; 2;

Bromine binding site 1 out of 2 in the Serial Femtosecond Crystallography (Sfx) of Ground State Bacteriorhodopsin Crystallized From Bicelles in Complex with HAD16 Determined Using 7-Kev X-Ray Free Electron Laser (Xfel) at Sacla


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 1 of Serial Femtosecond Crystallography (Sfx) of Ground State Bacteriorhodopsin Crystallized From Bicelles in Complex with HAD16 Determined Using 7-Kev X-Ray Free Electron Laser (Xfel) at Sacla within 5.0Å range: probe atom residue distance (Å) B Occ A:Br302 b:106.4 occ:0.30 BR1 A:7YH302 0.0 106.4 0.3 I1 A:7YH302 0.2 94.2 0.3 C4 A:7YH302 1.9 88.6 0.3 C2 A:7YH302 2.3 87.1 0.3 C5 A:7YH302 2.8 89.2 0.3 C3 A:7YH302 2.8 89.6 0.3 C3 A:7YH302 3.2 88.1 0.3 C1 A:7YH302 3.2 86.4 0.3 CD1 A:LEU22 3.7 78.3 1.0 C6 A:7YH302 4.1 91.2 0.3 C2 A:7YH302 4.1 89.4 0.3 CG A:LEU22 4.2 84.7 1.0 C4 A:7YH302 4.5 89.4 0.3 C6 A:7YH302 4.5 85.8 0.3 O A:LEU22 4.5 77.6 1.0 CB A:LEU22 4.6 70.5 1.0 C1 A:7YH302 4.7 84.8 0.3 C20 A:HP6314 4.8 138.6 0.7 CB A:TYR26 4.8 66.9 1.0 O26 A:7YH302 4.8 70.4 0.3 CD2 A:LEU25 4.9 107.9 1.0 CA A:LEU22 4.9 68.5 1.0

Bromine binding site 2 out of 2 in the Serial Femtosecond Crystallography (Sfx) of Ground State Bacteriorhodopsin Crystallized From Bicelles in Complex with HAD16 Determined Using 7-Kev X-Ray Free Electron Laser (Xfel) at Sacla


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 2 of Serial Femtosecond Crystallography (Sfx) of Ground State Bacteriorhodopsin Crystallized From Bicelles in Complex with HAD16 Determined Using 7-Kev X-Ray Free Electron Laser (Xfel) at Sacla within 5.0Å range: probe atom residue distance (Å) B Occ A:Br302 b:96.6 occ:0.30 BR1 A:7YH302 0.0 96.6 0.3 I1 A:7YH302 0.1 89.7 0.3 C4 A:7YH302 1.9 89.4 0.3 C2 A:7YH302 2.1 89.4 0.3 C3 A:7YH302 2.8 88.1 0.3 C5 A:7YH302 2.9 81.6 0.3 C3 A:7YH302 3.1 89.6 0.3 C1 A:7YH302 3.1 84.8 0.3 C2 A:7YH302 4.1 87.1 0.3 CG1 A:VAL217 4.1 69.4 1.0 C6 A:7YH302 4.2 85.8 0.3 CD2 A:TYR26 4.2 72.5 1.0 CA A:GLY23 4.2 66.1 1.0 CD1 A:LEU221 4.3 70.0 1.0 CB A:TYR26 4.3 66.9 1.0 C4 A:7YH302 4.4 88.6 0.3 C6 A:7YH302 4.4 91.2 0.3 CG A:TYR26 4.4 74.9 1.0 N A:GLY23 4.5 69.1 1.0 CD2 A:LEU221 4.6 73.1 1.0 O A:LEU22 4.6 77.6 1.0 C1 A:7YH302 4.6 86.4 0.3 C A:LEU22 4.7 70.1 1.0 CG A:LEU221 4.7 79.3 1.0 CE2 A:TYR26 4.9 70.7 1.0 C5 A:7YH302 4.9 89.2 0.3

S.Hanashima, T.Nakane, E.Mizohata. Heavy Atom Detergent/Lipid Combined X-Ray Crystallography For Elucidating the Structure-Function Relationships of Membrane Proteins. Membranes (Basel) V. 11 2021.
ISSN: ESSN 2077-0375
PubMed: 34832053
DOI: 10.3390/MEMBRANES11110823