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X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050
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X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050

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11:27 min

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May 13, 2020

DOI:

10.3791/61288-v

DOI:
10.3791/61288-v

•

11:27 min
May 13, 2020

•

2 Views
, , ,
1Laboratory of Microbiology, Department of Molecular Biology,Université Libre de Bruxelles, 2Labiris Institut de Recherche

Summary

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This protocol has been developed to study the dimer-dodecamer transition of TmPep1050, an M42 aminopeptidase, at the structural level. It is a straightforward pipeline starting from protein purification to X-ray data processing. Crystallogenesis, data set indexation, and molecular replacement have been emphasized through a case of study, TmPep1050H60A H307A variant.

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X-ray CrystallographyOligomeric StateThermotoga MaritimaAminopeptidaseTmPep1050Activity AssayApoenzyme PreparationDialysisUltrafiltration

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Cite this Article

Dutoit, R., Brandt, N., Van Elder, D., Droogmans, L. X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050. J. Vis. Exp. (159), e61288, doi:10.3791/61288 (2020).

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