Literature summary for 3.4.21.5 extracted from

Plavsa, J.J.; Rezacova, P.; Kugler, M.; Pachl, P.; Brynda, J.; Voburka, Z.; Celic, A.; Petri, E.T.; Skerlova, J.
In situ proteolysis of an N-terminal His tag with thrombin improves the diffraction quality of human aldo-keto reductase 1C3 crystals (2018), Acta Crystallogr. Sect. F, 74, 300-306 .

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Application

Application	Comment	Organism
additional information	a modified in situ proteolysis approach is applied to specifically remove the His tag by thrombin cleavage during crystallization screening trials. This improves the morphology and diffraction quality of the crystals and allowes the acquisition of high-resolution diffraction data and structure solution	Bos taurus

Organism

Organism	UniProt	Comment	Textmining
Bos taurus	P00735	prothrombin	-

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Release 2023.1 (January 2023)