DOI > 10.5291/ILL-DATA.8-01-365

This proposal is publicly available since 04/30/2018

Title

The Catalytic Mechanism of xylose isomerase

Abstract

Xylose isomerase (XI) is the most abundantly applied industrial enzyme, with major applications in the production of biofuels and value-added products from cellulosic biomass. Engineering efforts to improve the performance of XI will be significantly aided by understanding the enzyme's catalytic mechanism. Our goal is to use neutron crystallography to reveal the catalytic mechanism by determining the location and movement of H over the course of the multistep reaction. This involves determining a large number of neutron structures of XI in complex with different metals and substrates.In order to make this possible we have assembled an international consortium of scientists from ISIS, ILL, Fox Chase Cancer Center and LANSCE to collect these data sets on different beam lines. This consortium will not only be involved in determining the enzyme's mechanism but also in supporting the development of TOF protein crystallography at LMX at ISIS.

Experimental Report

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Data Citation

The recommended format for citing this dataset in a research publication is in the following format:

KEEN David A.; Matthew P. Blakeley; FORSYTH Victor Trevor; GLUSKER Jenny; HANSON Leif; Andrey Kovalevsky; LANGAN Paul; MASON, Sax A. and SAWADA Daisuke. (2013). The Catalytic Mechanism of xylose isomerase. Institut Laue-Langevin (ILL) doi:10.5291/ILL-DATA.8-01-365

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Metadata

Experiment Parameters

  • Environment temperature

    ambient
  • Experiment energy

    2.4
  • Experiment res energy

    ~1%

Sample Parameters

  • Formula

    • xylose isomerase amino acid
  • Consistence

    single crystal
  • Size

    50
  • Space

    I222
  • Unit cell A

    94
  • Unit cell B

    100
  • Unit cell C

    103
  • Container

    capillary