# Protein Energy Landscapes Determined by 5-Dimensional Crystallography

Source: [Protein Energy Landscapes Determined by 5-Dimensional Crystallography](<https://www.sota2.com/research/paper/68fa2c6f1e209131ce850220>)

Collection index: [llms.txt](<https://www.sota2.com/research/llms.txt>)

Data updated: 2025-10-24T15:20:53.977Z

Authors: Marius Schmidt, Vukica Srajer, Robert Henning, Hyotcherl Ihee, Namrta Purwar, Jason Tenboer, Shailesh Tripathi

Published: 2013-07-09T20:17:34.000Z

## Abstract

Free energy landscapes decisively determine the progress of enzymatically catalyzed reactions\[1\]. Time-resolved macromolecular crystallography unifies transient-state kinetics with structure determination \[2-4\] because both can be determined from the same set of X-ray data. We demonstrate here how barriers of activation can be determined solely from five-dimensional crystallography \[5\]. Directly linking molecular structures with barriers of activation between them allows for gaining insight into the structural nature of the barrier. We analyze comprehensive time series of crystal-lographic data at 14 different temperature settings and determine entropy and enthalpy contributions to the barriers of activation. 100 years after the discovery of X-ray scattering, we advance X-ray structure determination to a new frontier, the determination of energy landscapes.

## Recorded benchmark results

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## Original sources and implementation

[Original paper](<https://arxiv.org/abs/1307.2588>)

[PDF](<https://arxiv.org/pdf/1307.2588.pdf>)