Despite their biological importance, few methods exist to monitor these complexes as they assemble, dissociate or function. The ability to observe these dynamics in action will present new strategies for manipulating gene expression.

LapD then, through its periplasmic domains, binds to enzyme LapG, which keeps LapG from breaking down the molecule responsible for the biofilm assembly, the elastin LapA.

A few years ago the Sondermann group used MacCHESS facilities to solve several molecular structures of cytoplasmic domains of the LapD regulatory protein from Pseudomonas fluorescens, alone and in complex with signaling molecule cdGMP. (Navarro, et al., 2011 DOI 10.1371/JOURNAL.PBIO.1000588)

Over the course of three days, the teachers participated in a variety of lessons and activities geared towards basic engineering, problem solving and scientific thinking. This Science Snapshot provided teachers with ideas and activities to better implement the principles of engineering in their classrooms, and allowed them to dry-run prepared materials. The focus of their investigations? To eventually design and build a device to measure light penetration. The teachers were then able to test their designs in Cayuga Lake aboard the Floating Classroom.

High-quality epitaxial thin films are key components of almost all modern electronic devices. During epitaxial thin film growth, lattice mismatch between the substrate and the film generates elastic strain, which eventually leads to defects that relieve the strain beyond certain thicknesses of film growth.

Microfluidic mixing chips are used by scientists to analyze biological molecules. They have small channels in which biological solutions, usually solutions of protein, are mixed. Biological small angle x-ray solution scattering (BioSAXS) is then used to study how these biomolecules change under different conditions, for example when they mix with hormones and drugs or when they interact with other biomolecules. These observations can help further our understanding of how cells function.

Long duration (tens of minutes to hours) X-ray beam position shifts have been present due to warm-ups after beam interruptions and as a result of changes due to the temperature shift of the CESR environment. These beam position shifts, especially during start-up times could be as large as hundreds of microns and the warm-up time as long as 12 hours.

Joint efforts made by scientists across Cornell campus from the Departments of Chemical and Biological Engineering, Material Sciences and Engineering, and the Cornell High Energy Synchrotron Source (CHESS) have resulted to a novel and feasible tool in which a nanocrystal superlattice is used as a nanoscopic pressure cell for in-situ investigation of soft molecules under pressure.

As an innovative tool for exploiting matter with atomic precision, X-ray based crystallography served as ways to solve the scientific controversies such as the molecular ordering of planar benzene, the existence of ionic crystals and the determination of complex macromolecular structures.

Gillilan, together with a former MacCHESS postdoc, Soren Skou and long time CHESS user, Nozomi Ando have distilled much of their knowledge into a Nature Protocols article.