Protein crystallography at the Brazilian Synchrotron Light Source-LNLS (1996)
- Authors:
- USP affiliated authors: OLIVA, GLAUCIUS - IFSC ; CASTELLANO, EDUARDO ERNESTO - IFSC ; GARRATT, RICHARD CHARLES - IFSC
- Unidade: IFSC
- Assunto: MATÉRIA CONDENSADA
- Language: Inglês
- Imprenta:
- Publisher: Argone National Laboratory
- Publisher place: Argonne
- Date published: 1996
- Source:
- Título do periódico: Synchrotron Radiation Satellite Meeting
- Conference titles: Synchrotron Radiation Satellite Meeting
-
ABNT
OLIVA, Glaucius et al. Protein crystallography at the Brazilian Synchrotron Light Source-LNLS. 1996, Anais.. Argonne: Argone National Laboratory, 1996. . Acesso em: 19 set. 2024. -
APA
Oliva, G., Castellano, E. E., Garratt, R. C., Guimarães, B. G., Craievich, A., Polikarpov, I., & Arruda, P. (1996). Protein crystallography at the Brazilian Synchrotron Light Source-LNLS. In Synchrotron Radiation Satellite Meeting. Argonne: Argone National Laboratory. -
NLM
Oliva G, Castellano EE, Garratt RC, Guimarães BG, Craievich A, Polikarpov I, Arruda P. Protein crystallography at the Brazilian Synchrotron Light Source-LNLS. Synchrotron Radiation Satellite Meeting. 1996 ;[citado 2024 set. 19 ] -
Vancouver
Oliva G, Castellano EE, Garratt RC, Guimarães BG, Craievich A, Polikarpov I, Arruda P. Protein crystallography at the Brazilian Synchrotron Light Source-LNLS. Synchrotron Radiation Satellite Meeting. 1996 ;[citado 2024 set. 19 ] - Protein crystallography in Brazil
- Set-up and experimental parameters of the protein crystallography beamline at the Brazilian National Synchrotron Laboratory
- Protein crystallography station at LNLS
- Estacao experimental de cristalografia de proteinas do lns
- Protein crystallography beamline at lnls
- Protein crystallography station at LNLS
- Crystal and molecular structure of bromo bis (1-phenyl-3,5-dimethylpyrazole) copper (i), 'CU''BR'' (PDMP) IND.2'
- Electron density rigid-body refinement
- Refinement and temperature factor analysis of the r-state m15-c118, 239s double-mutant of the enzyme glucosamine-6-phosphate deaminase from escherichia coli k12
- Enzymatic mechanism and allosteric regulation of glucosamine-6-phosphate deaminase from escherichia colli
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