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Structural Biology

Structure Determination

Modern life science would be unthinkable without methods to precisely determine the three-dimensional structure of the involved macromolecules. Our recent advances in technology, and ease-of-use have accelerated the speed of research and impressively increased global success rates, leading to more patents and publications than ever before.

Proteins and their complexes are involved in almost all cellular processes, including metabolism, cell signaling and differentiation, and reproduction. Understanding these processes at the molecular level requires a detailed understanding the structures of the proteins themselves.

Single crystal X-ray diffraction (SC-XRD) remains the most productive technique for determining the structures of proteins and their complexes. The determination of protein structures is a labor-intensive process, and so development of home-lab SC-XRD instruments that accelerate the production and characterization of diffraction quality crystals is key to successful research. Several 100 KDa

In situ crystallography enables the analysis of crystals directly in the lab and has such has seen a rise in use due to the ability to optimize crystal growth conditions more quickly.
NMR is a technique used in all Structural Biology departments to provide a dynamic complement to the structures determined by SC-XRD.

Ground-breaking crystallography has always been driven by the development of improved tools. This is evident at synchrotron facilities where current beamline upgrades are seeing the introduction of microfocus beams, faster mixed mode photon-counting detectors, data-processing pipelines, and multi-axis goniometers.
Bringing these possibilities to the home lab has been Bruker’s driving vision for the D8 QUEST and D8 VENTURE, our new D8 Structural Biology Solutions.