Source: Collected Abstracts. Conference titles: Congress of the International Union of Crystallography. Unidade: IFSC
Subjects: ESTEREOQUÍMICA, QUÍMICA ANALÍTICA INSTRUMENTAL, MEDICAMENTO
ABNT
EMSLEY, J et al. Three dimensional structure of human serum amyloid p-component defined at 2.0'ANGSTRON' reveals a lectin like fold and calcium mediated ligand binding. 1993, Anais.. Beijing: Instituto de Física de São Carlos, Universidade de São Paulo, 1993. . Acesso em: 24 ago. 2024.APA
Emsley, J., White, H. E., Oliva, G., O'hara, B. P., Wood, S. P., Tickle, I. J., et al. (1993). Three dimensional structure of human serum amyloid p-component defined at 2.0'ANGSTRON' reveals a lectin like fold and calcium mediated ligand binding. In Collected Abstracts. Beijing: Instituto de Física de São Carlos, Universidade de São Paulo.NLM
Emsley J, White HE, Oliva G, O'hara BP, Wood SP, Tickle IJ, Pepys MB, Blundell TL. Three dimensional structure of human serum amyloid p-component defined at 2.0'ANGSTRON' reveals a lectin like fold and calcium mediated ligand binding. Collected Abstracts. 1993 ;[citado 2024 ago. 24 ]Vancouver
Emsley J, White HE, Oliva G, O'hara BP, Wood SP, Tickle IJ, Pepys MB, Blundell TL. Three dimensional structure of human serum amyloid p-component defined at 2.0'ANGSTRON' reveals a lectin like fold and calcium mediated ligand binding. Collected Abstracts. 1993 ;[citado 2024 ago. 24 ]