Journal:Acta Cryst D:S2059798319009008
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<b>Molecular Tour</b><br> | <b>Molecular Tour</b><br> | ||
| + | Solving a protein crystal structure without a homologous template involves experimental phasing. Ultimately, this requires the incorporation of heavy atoms into the lattice of the protein crystal. However, this process can be very laborious as suitable heavy atom compounds and conditions are found empirically through screening. A method to efficiently derivatize crystals was developed, by performing a Random Microseed Matrix screen (rMMS) in the presence of I3C. | ||
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| + | 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 (5-amino-2,4,6-triiodoisophthalic acid) is compatible with many crystallization reagents and provides a large phasing power. | ||
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| + | In the two test proteins, the Orf11 NTD from Staphylococcus phage P68 and Hen Egg White Lysozyme, 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. | ||
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| + | 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. | ||
<b>References</b><br> | <b>References</b><br> | ||
Revision as of 11:24, 26 June 2019
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