Sandalova, T.; Sala, B.M.; Moche, M.; Ljunggren, H.-G.; Alici, E.; Henriques-Normark, B.; Agback, T.; Lesovoy, D.; Agback, P.; Achour, A.
Crystallographic and NMR Study of Streptococcus pneumonia LCP Protein PsrSp Indicate the Importance of Dynamics in Four Long Loops for Ligand Specificity. Crystals 2024, 14, 1094.
https://doi.org/10.3390/cryst14121094
AMA Style
Sandalova T, Sala BM, Moche M, Ljunggren H-G, Alici E, Henriques-Normark B, Agback T, Lesovoy D, Agback P, Achour A.
Crystallographic and NMR Study of Streptococcus pneumonia LCP Protein PsrSp Indicate the Importance of Dynamics in Four Long Loops for Ligand Specificity. Crystals. 2024; 14(12):1094.
https://doi.org/10.3390/cryst14121094
Chicago/Turabian Style
Sandalova, Tatyana, Benedetta Maria Sala, Martin Moche, Hans-Gustaf Ljunggren, Evren Alici, Birgitta Henriques-Normark, Tatiana Agback, Dmitry Lesovoy, Peter Agback, and Adnane Achour.
2024. "Crystallographic and NMR Study of Streptococcus pneumonia LCP Protein PsrSp Indicate the Importance of Dynamics in Four Long Loops for Ligand Specificity" Crystals 14, no. 12: 1094.
https://doi.org/10.3390/cryst14121094
APA Style
Sandalova, T., Sala, B. M., Moche, M., Ljunggren, H.-G., Alici, E., Henriques-Normark, B., Agback, T., Lesovoy, D., Agback, P., & Achour, A.
(2024). Crystallographic and NMR Study of Streptococcus pneumonia LCP Protein PsrSp Indicate the Importance of Dynamics in Four Long Loops for Ligand Specificity. Crystals, 14(12), 1094.
https://doi.org/10.3390/cryst14121094