Next Article in Journal
Hardness-Depth Relationship with Temperature Effect for Single Crystals—A Theoretical Analysis
Next Article in Special Issue
Serial Crystallography: Preface
Previous Article in Journal
Effects of Pulsed Magnetic Fields of Different Intensities on Dislocation Density, Residual Stress, and Hardness of Cr4Mo4V Steel
Open AccessReview

Reaction Initiation in Enzyme Crystals by Diffusion of Substrate

Physics Department, University of Wisconsin-Milwaukee, Milwaukee, WI 53211, USA
Crystals 2020, 10(2), 116; https://doi.org/10.3390/cryst10020116
Received: 9 January 2020 / Revised: 4 February 2020 / Accepted: 7 February 2020 / Published: 13 February 2020
(This article belongs to the Special Issue Macromolecular Serial Crystallography)
Ever since the first structure of an enzyme, lysozyme, was solved, scientists have been eager to explore how these molecules perform their catalytic function. There has been an overwhelmingly large body of publications that report the X-ray structures of enzymes determined after substrate and ligand binding. None of them truly show the structures of an enzyme working freely through a sequence of events that range from the formation of the enzyme–substrate complex to the dissociation of the product. The technical difficulties were too severe. By 1969, Sluyterman and de Graaf had pointed out that there might be a way to start a reaction in an enzyme crystal by diffusion and following its catalytic cycle in its entirety with crystallographic methods. The crystal only has to be thin enough so that the diffusion is not rate limiting. Of course, the key questions are as follows: How thin should the crystal be? Will the existing X-ray sources be able to collect data from a thin enough crystal fast enough? This review shines light on these questions.
Keywords: time-resolved crystallography; enzymology; mix-and-inject serial crystallography; X-ray free electron lasers; diffraction before destruction time-resolved crystallography; enzymology; mix-and-inject serial crystallography; X-ray free electron lasers; diffraction before destruction
MDPI and ACS Style

Schmidt, M. Reaction Initiation in Enzyme Crystals by Diffusion of Substrate. Crystals 2020, 10, 116.

Show more citation formats Show less citations formats
Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Article Access Map by Country/Region

1
Back to TopTop