Crystallization and preliminary X-ray crystallographic studies on maltosyltransferase from Thermotoga maritima

Jacky Burke, Anna Roujeinikova, Patrick J. Baker, Svetlana Sedelnikova, Carsten Raasch, Wolfgang Liebl, David W. Rice

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4 Citations (Scopus)

Abstract

Thermotoga maritima maltosyltransferase (MTase) is a 73.7 kDa molecular weight amylolytic enzyme which catalyzes the transfer of maltosyl units from maltodextrins or starch to suitable acceptors. Crystals of recombinant MTase have been obtained by the hanging-drop vapour-diffusion method using ammonium phosphate as a precipitating agent. The crystals belong to space group P4122 or its enantiomorph P4322, with unit-cell parameters a = b = 148.7, c = 106.7 Å. The asymmetric unit appears to contain one subunit, corresponding to a very low packing density of 4.0 Å3 Da-1. The crystals diffract X-rays to at least 2.4 Å resolution on a synchrotron-radiation source.

Original languageEnglish
Pages (from-to)1049-1050
Number of pages2
JournalActa Crystallographica Section D: Biological Crystallography
Volume56
Issue number8
DOIs
Publication statusPublished - 2000
Externally publishedYes

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