Abstract
One of the most frequent problems in crystallization is poor quality of the crystals. In order to overcome this obstacle several methods have been utilized, including amino-acid substitutions of the target protein. Here, an example is presented of crystal-quality improvement by leucine-to-methionine substitutions. A variant protein with three amino-acid substitutions enabled improvement of the crystal quality of the histone chaperone SET/TAF-Iβ/ INHAT when combined with optimization of the cryoconditions. This procedure improved the resolution of the SET/TAF-Iβ/INHAT crystals from around 5.5 to 2.3 Å without changing the crystallization conditions. © International Union of Crystallography 2008.
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Senda, M., Muto, S., Horikoshi, M., & Senda, T. (2008). Effect of leucine-to-methionine substitutions on the diffraction quality of histone chaperone SET/TAF-Iβ/INHAT crystals. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 64(10), 960–965. https://doi.org/10.1107/S1744309108028704
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