Creating LaTeX documents from within Stata using texdoc

This paper discusses the use of -texdoc- for creating LaTeX documents from within Stata. Specifically, -texdoc- provides a way to embed LaTeX code directly in a do-file and to automate the integration of results from Stata in the final document. The command can be used, for example, to assemble automatic reports, write a Stata Journal article, prepare slides for classes, or put together solutions for homework assignments.

Creating LaTeX documents from within Stata

In this presentation, I present a new user package called texdoc. texdoc can be used to create a LaTeX document from within Stata in a weaving fashion. This is especially useful if you want to produce a LaTeX document that contains Stata output, such as a Stata Journal article or solutions to statistics homework assignments. I will provide examples illustrating the usage of texdoc.

Generador de exámenes test aleatorios basados en R y LATEX

El presente documento aborda el proceso de realización del proyecto \Generación aleatoria de Test" utilizando para ello un gestor de base de datos y principalmente los lenguajes LaTex y R. También se realizará una explicación de cómo se han integrado entre s ambos lenguajes relacionándolos con la base de datos, cómo se han codificado los métodos empleados para la realización del sistema de test, los problemas que han ido surgiendo a lo largo de dicha integración y desarrollo y las mejores medidas que se han adoptado para tratar de solventarlos. Por último, se ilustraran unos ejemplos de instalación y funcionamiento del programa y se comentaran unas breves conclusiones obtenidas tras su finalización y las posibles líneas futuras que se pueden adoptar de cara a progresar y mejorar el programa.

Characterization of Euphorbia characias Latex Amine Oxidase1

A copper-containing amine oxidase from the latex of Euphorbia characias was purified to homogeneity and the copper-free enzyme obtained by a ligand-exchange procedure. The interactions of highly purified apo- and holoenzyme with several substrates, carbonyl reagents, and copper ligands were investigated by optical spectroscopy under both aerobic and anaerobic conditions. The extinction coefficients at 278 and 490 nm were determined as 3.78 × 105 m−1 cm−1 and 6000 m−1 cm−1, respectively. Active-site titration of highly purified enzyme with substrates and carbonyl reagents showed the presence of one cofactor at each enzyme subunit. In anaerobiosis the native enzyme oxidized one equivalent substrate and released one equivalent aldehyde per enzyme subunit. The apoenzyme gave exactly the same 1:1:1 stoichiometry in anaerobiosis and in aerobiosis. These findings demonstrate unequivocally that copper-free amine oxidase can oxidize substrates with a single half-catalytic cycle. The DNA-derived protein sequence shows a characteristic hexapeptide present in most 6-hydroxydopa quinone-containing amine oxidases. This hexapeptide contains the tyrosinyl residue that can be modified into the cofactor 6-hydroxydopa quinone.

Programas de Cálculo Científico y Procesamiento de Textos: LaTeX. Práctica 1

Ejercicios LaTeX Sesión 1

Programas de Cálculo Científico y Procesamiento de Textos: LaTeX. Práctica 2

Ejercicios LaTeX Sesión 2

Programas de Cálculo Científico y Procesamiento de Textos: LaTeX. Práctica 3

Ejercicios LaTeX Sesión 3