Small angle x-ray scattering reveals conformational and oligomerization form changes in pig S100A12 (1999)
- Authors:
- USP affiliated authors: GARRATT, RICHARD CHARLES - IFSC ; JESUS, WANDA DRAGHETTA PERUSSI DE - IFSC ; OLIVA, GLAUCIUS - IFSC ; SCULACCIO, SUSANA ANDREA - IFSC
- Unidade: IFSC
- Subjects: BIOLOGIA MOLECULAR; MACROMOLÉCULA
- Language: Inglês
- Imprenta:
- Source:
- Título: Abstracts
- Conference titles: Congress and General Assembly of the International Union of Crystallography
-
ABNT
NONATO, Maria Cristina et al. Small angle x-ray scattering reveals conformational and oligomerization form changes in pig S100A12. 1999, Anais.. Glasgow: Instituto de Física de São Carlos, Universidade de São Paulo, 1999. . Acesso em: 27 dez. 2025. -
APA
Nonato, M. C., Jesus, W. D. P. de, Sculaccio, S. A., Garratt, R. C., Oliva, G., Barberato, C., et al. (1999). Small angle x-ray scattering reveals conformational and oligomerization form changes in pig S100A12. In Abstracts. Glasgow: Instituto de Física de São Carlos, Universidade de São Paulo. -
NLM
Nonato MC, Jesus WDP de, Sculaccio SA, Garratt RC, Oliva G, Barberato C, Schleicher C, Santome JA. Small angle x-ray scattering reveals conformational and oligomerization form changes in pig S100A12. Abstracts. 1999 ;[citado 2025 dez. 27 ] -
Vancouver
Nonato MC, Jesus WDP de, Sculaccio SA, Garratt RC, Oliva G, Barberato C, Schleicher C, Santome JA. Small angle x-ray scattering reveals conformational and oligomerization form changes in pig S100A12. Abstracts. 1999 ;[citado 2025 dez. 27 ] - Structural studies on calgranulin C, a S100 calcium binding protein from pig granulocytes
- Cristalizacao de novas proteinas em sao carlos
- Crystallographic studies of the glutamate specific endopeptidase from Bacillus licheniformis
- Analise cristalografica da anidrase carbonica bovina nativa
- 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
- Determinacao estrutural da anidrase carbonica bovina
- Calmodulin from canavalis ensiformis seeds-effect of calcium on electroforetic mobility, protein conformation and folding
- Crystallization and preliminary crystallographic studies of bovine carbonic anhydrase
- The refined crystal structure of carbonic anhydrase from bovine erythrocytes at 2.5 'ANGSTRON' resolution
- 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
How to cite
A citação é gerada automaticamente e pode não estar totalmente de acordo com as normas
