Accepted_test

Screening for crystallization conditions of ruminant’s chymosins

Authors:
Mironova Еkaterina, SRF \"SKIF\"
Belenkaya Svetlana, Center of Virology and Biotechnology «Vector»
Shcherbakov Dmitry, The State Research Center of Virology and Biotechnology «Vector»
Borshchevskiy Valentin, Moscow Institute of Physics and Technology
Arkhipov Sergey, SRF \"SKIF\"
Kolybalov Dmitry, SRF \"SKIF\"
Volosnikova Ekaterina, The State Researc Center of Virology and Biotechnology «Vector»\"

Abstract ID: 529

Event: BGRS-abstracts

Sections: [Sym 3] Section “Structural biology of proteins nucleic acids and membranes”

Chymosin, a peptidase protein widely used in the food industry, exhibits varying specificity to cow's milk kappa casein across different ruminant species. This study aimed to identify crystallization conditions for chymosins from Altai maral, elk, argali, and reindeer for X-ray diffraction analysis to elucidate their mechanisms of action and substrate specificity. Crystallization was conducted using the sitting-drop method and commercially available screening kits, with X-ray diffraction analysis performed on the maral chymosin. Successful crystallization conditions were identified for maral, elk, and argali chymosins, with the crystal structure of maral chymosin being deciphered and deposited. However, further research is needed to determine the crystallization conditions for reindeer chymosin. This study was supported by a budget project of the Ministry of Science and Higher Education of the Russian Federation for Synchrotron radiation facility SKIF, Boreskov Institute of Catalysis (FWUR-2024-0042)