Molecular replacement at its limits? the structure determination of t. Cruzi g-glyceraldehyde-3-phosphate dehydrogenase, 12 monomers in the asymmetric unit and 41% data completeness at 3.5'ANGSTRON' resolution (1996)
- Authors:
- USP affiliated authors: JESUS, WANDA DRAGHETTA PERUSSI DE - IFSC ; OLIVA, GLAUCIUS - IFSC
- Unidade: IFSC
- Subjects: PROTEÍNAS; ENZIMAS; BIOLOGIA MOLECULAR
- Language: Inglês
- Imprenta:
- Source:
- Título do periódico: Resumos
- Conference titles: Encontro Nacional de Fisica da Materia Condensada
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ABNT
GUIMARAES, B G et al. Molecular replacement at its limits? the structure determination of t. Cruzi g-glyceraldehyde-3-phosphate dehydrogenase, 12 monomers in the asymmetric unit and 41% data completeness at 3.5'ANGSTRON' resolution. 1996, Anais.. São Paulo: Sbf, 1996. . Acesso em: 24 abr. 2024. -
APA
Guimaraes, B. G., Souza, D. H. F., Jesus, W. D. P., & Oliva, G. (1996). Molecular replacement at its limits? the structure determination of t. Cruzi g-glyceraldehyde-3-phosphate dehydrogenase, 12 monomers in the asymmetric unit and 41% data completeness at 3.5'ANGSTRON' resolution. In Resumos. São Paulo: Sbf. -
NLM
Guimaraes BG, Souza DHF, Jesus WDP, Oliva G. Molecular replacement at its limits? the structure determination of t. Cruzi g-glyceraldehyde-3-phosphate dehydrogenase, 12 monomers in the asymmetric unit and 41% data completeness at 3.5'ANGSTRON' resolution. Resumos. 1996 ;[citado 2024 abr. 24 ] -
Vancouver
Guimaraes BG, Souza DHF, Jesus WDP, Oliva G. Molecular replacement at its limits? the structure determination of t. Cruzi g-glyceraldehyde-3-phosphate dehydrogenase, 12 monomers in the asymmetric unit and 41% data completeness at 3.5'ANGSTRON' resolution. Resumos. 1996 ;[citado 2024 abr. 24 ] - Molecular replacement at its limits? the structure determination of t. Cruzi g- glyceraldehyde -3-phosphate dehydrogenase, 12 monomers in the asymmetric unit and 41% data completeness at 3.5'ANGSTRON' resolution
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