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Crystallization and preliminary crystallographic analysis of human L-xylulose reductase. | LitMetric

Crystallization and preliminary crystallographic analysis of human L-xylulose reductase.

Acta Crystallogr D Biol Crystallogr

Department of Medicinal Chemistry, Victorian College of Pharmacy, Monash University(Parkville Campus), Parkville, Victoria 3052, Australia.

Published: August 2002

AI Article Synopsis

  • The study describes the crystallization of human L-xylulose reductase using a hanging-drop vapor-diffusion technique, resulting in high-quality crystals.
  • The obtained crystals can diffract X-rays to a resolution of 2.1 Å and fall into the orthorhombic P222 space group, with specific unit-cell dimensions.
  • This is the first documented case of crystallizing a xylulose reductase that is the same as diacetyl reductase, indicating a significant advancement in understanding this enzyme.

Article Abstract

Human L-xylulose reductase was crystallized from buffered polyethylene glycol solutions using the hanging-drop vapour-diffusion method. The crystals diffract to 2.1 A resolution and belong to the orthorhombic P222 space group, with unit-cell parameters a = 72.9, b = 74.1, c = 87.9 A. This is the first crystallization report of a xylulose reductase that is identical to diacetyl reductase.

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Source
http://dx.doi.org/10.1107/s0907444902008156DOI Listing

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