6Z02

Photosynthetic Reaction Center From Rhodobacter Sphaeroides strain RV in surfo crystallization

Summary for 6Z02

• Entry DOI: 10.2210/pdb6z02/pdb
• Related: 3V3Y
• Descriptor: Reaction center protein H chain, POTASSIUM ION, BACTERIOCHLOROPHYLL A, ... (20 entities in total)
• Functional Keywords: photosynthetic reaction center, bacteriochlorophyll, rhodobacter sphaeroides, serial crystallography, mesophase crystallization, lipid sponge phase, lipid cubic phase, spheroidene, ubiquinone, photosynthesis
• Biological source: Rhodobacter sphaeroides; More
• Total number of polymer chains: 3
• Total formula weight: 105776.37

Authors

Gabdulkhakov, A.G.,Selikhanov, G.K.,Fufina, T.Y.,Vasilieva, L.G.,Betzel, C. (deposition date: 2020-05-07, release date: 2020-12-02, Last modification date: 2024-01-24)

Primary citation

Selikhanov, G.,Fufina, T.,Vasilieva, L.,Betzel, C.,Gabdulkhakov, A.
Novel approaches for the lipid sponge phase crystallization of the Rhodobacter sphaeroides photosynthetic reaction center.
Iucrj, 7:1084-1091, 2020

PubMed Abstract: With the recent developments in the field of free-electron-laser-based serial femtosecond crystallography, the necessity to obtain a large number of high-quality crystals has emerged. In this work crystallization techniques were selected, tested and optimized for the lipid mesophase crystallization of the membrane pigment-protein complex, known as the photosynthetic reaction center (RC). Novel approaches for lipid sponge phase crystallization in comparatively large volumes using Hamilton gas-tight glass syringes and plastic pipetting tips are described. An analysis of RC crystal structures obtained by lipid mesophase crystallization revealed non-native ligands that displaced the native electron-transfer cofactors (carotenoid sphero-idene and a ubi-quinone molecule) from their binding pockets. These ligands were identified and were found to be lipids that are major mesophase components. The selection of distinct co-crystallization conditions with the missing cofactors facilitated the restoration of sphero-idene in its binding site.

PubMed: 33209319
DOI: 10.1107/S2052252520012142

Experimental method

X-RAY DIFFRACTION (2.1 Å)