Crystallization and preliminary X-ray diffraction analysis of haloalkane dehalogenase linB from Sphingomonas paucimobilis UT26

Ivana Smatanová, Yuji Nagata, L. Anders Svensson, Masamichi Takagi, Jaromír Marek

Research output: Contribution to journalArticle

10 Citations (Scopus)

Abstract

Haloalkane hydrolytic dehalogenase LinB from Sphingomonas paucimobilis UT26, an enzyme which releases chloride or bromide anion from n-halogenated alkanes and has a broad range of substrate specificity, was crystallized using the hanging-drop vapour-diffusion method at 278 K. The best crystals were obtained by microseeding with a precipitant containing 18-20%(w/v) PEG 6000, 0.2 M calcium acetate and 0.1 M Tris-HCl pH 8.9. The crystals diffract to at least 1.60 Å using synchrotron X-ray under cryogenic (100 K) conditions. They belong to the orthorhombic space group P21212 with unit-cell parameters a = 50.29, b = 71.70, c = 72.73 Å. The asymmetric unit contains one molecule of the enzyme.

Original languageEnglish
Pages (from-to)1231-1233
Number of pages3
JournalActa Crystallographica Section D: Biological Crystallography
Volume55
Issue number6
DOIs
Publication statusPublished - 1999 Jun 1
Externally publishedYes

ASJC Scopus subject areas

  • Structural Biology

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