Herein, we present KiMoPack, an analysis tool for the ki netic mo deling of transient spectroscopic data. KiMoPack enables a state-of-the-art analysis routine including data preprocessing and standard fitting (global analysis), as well as fitting of complex (target) kinetic models, interactive viewing of (fit) results, and multiexperiment analysis via user accessible functions and a graphical user interface (GUI) enhanced interface. To facilitate its use, this paper guides the user through typical operations covering a wide range of analysis tasks, establishes a typical workflow and is bridging the gap between ease of use for less experienced users and introducing the advanced interfaces for experienced users. KiMoPack is open source and provides a comprehensive front-end for preprocessing, fitting and plotting of 2-dimensional data that simplifies the access to a powerful -based data-processing system and forms the foundation for a well documented, reliable, and reproducible data analysis.

Ambient pressure X-ray photoelectron spectroscopy (APXPS) can provide a compelling platform for studying an analyte's oxidation and reduction reactions in a solution. This paper presents proof-of-principle operando measurements of a model organometallic complex, iron hexacyanide, in an aqueous solution using the dip-and-pull technique. The data demonstrates that the electrochemically active liquid meniscus on the working electrode can undergo controlled redox reactions, which were observed using APXPS. A detailed discussion of several critical experimental considerations is included as guidance for anyone undertaking comparable experiments.

Investigating the optical properties of various chemical compounds using UV–vis spectrophotometers is an essential part of education in chemistry. However, commercial spectrophotometers are usually treated as “magic black boxes”, where the dominant majority of optical elements are hidden “under the hood”. This often limits understanding of the mechanisms behind the generation of spectral curves, which in turn may impede the ability to understand the limitations of the applied method and, in some cases, interpret the acquired data. In addition, the study of optical emission phenomena using fluorescence spectrophotometers is seldom implemented in educational laboratories due to the practical challenges and costs of the devices, which severely limit pedagogic access to this topic. For students to be more confident with these two basic spectroscopy techniques, we have developed a laboratory kit that provides a multifaceted learning experience. Starting with a basic exploration of an instrument assembly, it teaches, for example, such technical concepts as spectral resolution and detection sensitivity. More fundamentally, it enables deeper learning of the Beer–Lambert law and the notion of Stokes shift. The spectrophotometer is built from cost-efficient materials and is easily scalable, making it affordable for many educational laboratories. Due to a modular design, it is adaptable to various levels of education and has been successfully applied during high school-, undergraduate-, and graduate-level classes.

The structure and function of proteins are strongly affected by the surrounding solvent water, for example through hydrogen bonds and the hydrophobic effect. These interactions depend not only on the position, but also on the orientation, of the water molecules around the protein. Therefore, it is often vital to know the detailed orientations of the surrounding ordered water molecules. Such information can be obtained by neutron crystallography. However, it is tedious and time-consuming to determine the correct orientation of every water molecule in a structure (there are typically several hundred of them), which is presently performed by manual evaluation. Here, a method has been developed that reliably automates the orientation of a water molecules in a simple and relatively fast way. Firstly, a quantitative quality measure, the real-space correlation coefficient, was selected, together with a threshold that allows the identification of water molecules that are oriented. Secondly, the refinement procedure was optimized by varying the refinement method and parameters, thus finding settings that yielded the best results in terms of time and performance. It turned out to be favourable to employ only the neutron data and a fixed protein structure when reorienting the water molecules. Thirdly, a method has been developed that identifies and reorients inadequately oriented water molecules systematically and automatically. The method has been tested on three proteins, galectin-3C, rubredoxin and inorganic pyrophosphatase, and it is shown that it yields improved orientations of the water molecules for all three proteins in a shorter time than manual model building. It also led to an increased number of hydrogen bonds involving water molecules for all proteins.