Journal:Acta Cryst D:S2059798319009008
From Proteopedia
Combining rMMS and the Magic Triangle for the efficient structure solution of a bacteriophage P68 lysinJia Quyen Truong, Santosh Panjikar, Linda Shearwin, John Bruning and Keith Shearwin [1] Molecular Tour In a random microseed matrix, a crystal or crystalline precipitate is crushed up, diluted and added to new crystallization conditions from a sparse matrix screen. This often generates new crystallization where crystals can grow. I3C is compatible with many crystallization reagents and provides a large phasing power. In the two test proteins, the from Staphylococcus phage P68 (PDB entry 6o43) and (PDB entry 6pbb), the rMMS technique in the presence of I3C generated numerous new conditions where derivatized crystals could grow. The I3C molecules in the lattice were sufficient to completely solve the structure using anomalous phasing methods. I3C was present in the tested crystals in the rMMS screens containing I3C, where they often sit at the junctions between protein molecules in the lattice. These bridging contacts could improve the crystal lattice or generate new conditions where crystals can grow. I3C can mediate contacts between protein molecules in a crystal:
The same I3C molecule from the Orf11 NTD crystal is displayed in two different orientations for clarity. I3C-protein interactions include hydrogen bonding, π-π stacking interactions, salt bridges, water bridges and halogen bonding. In both cases, each I3C molecule forms interactions with three different proteins molecules (each shown in a different color), which could assist in lattice packing. PDB references: Crystal structure of a lysin protein from Staphylococcus phage P68 6o43; Crystal structure of Hen Egg White Lysozyme in complex with I3C 6pbb. References
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