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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.
Acta Crystallographica Section F – Wiley
Published: Oct 1, 2008
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