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Title

Humidity control can compensate for the damage induced in protein crystals by alien solutions

AuthorsAbad-Zapatero, Cele; Guasch, Alicia
Issue Date2011
PublisherInternational Union of Crystallography
CitationActa Crystallographica Section F 67(10): 1300-1308 (2011)
AbstractThe use of relative humidity control of protein crystals to overcome some of the shortcomings of soaking ligands (i.e. inhibitors, substrate analogs, weak ligands) into pre-grown apoprotein crystals has been explored. Crystals of PurE (EC 4.1.1.21), an enzyme from the purine-biosynthesis pathway of Bacillus anthracis, were used as a test case. The findings can be summarized as follows: (i) using humidity control, it is possible to improve/optimize the diffraction quality of crystals soaked in solutions of organic solvent (DMSO, ethanol) containing ligands/inhibitors; (ii) optimization of the relative humidity can compensate for the deterioration of the diffraction pattern that is observed upon desalting crystals grown in high salt; (iii) combining desalting protocols with the addition of PEG it is possible to achieve very high concentrations of weak ligands (in the 5-10 mM range) in soaking solutions and (iv) fine control of the relative humidity of crystals soaked in these solutions can compensate for the deterioration of crystal diffraction and restore high-resolution diffraction for structure-based and fragment-based drug design. It is suggested that these experimental protocols may be useful in other protein systems and may be applicable in academic or private research to increase the probability of obtaining structures of protein-ligand complexes at high resolution. © 2011 International Union of Crystallography All rights reserved.
Descriptionet al.
Publisher version (URL)http://dx.doi.org/10.1107/S174430911103377X
URIhttp://hdl.handle.net/10261/53113
DOI10.1107/S174430911103377X
Identifiersdoi: 10.1107/S174430911103377X
issn: 1744-3091
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