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

• Published in: Acta crystallographica. Section D, Biological crystallography. Vol. 56; no. 8; pp. 1049 - 1050
• Main Authors: Burke, Jacky, Roujeinikova, Anna, Baker, Patrick J., Sedelnikova, Svetlana, Raasch, Carsten, Liebl, Wolfgang, Rice, David W.
• Format: Journal Article
• Language: English
• Published: 5 Abbey Square, Chester, Cheshire CH1 2HU, England Munksgaard International Publishers 01.08.2000
• Subjects: Crystallization; Crystallography, X-Ray; Escherichia coli - genetics; Glycogen Debranching Enzyme System - chemistry; Glycogen Debranching Enzyme System - genetics; hyperthermophiles; Recombinant Proteins - chemistry; Recombinant Proteins - genetics; Thermotoga maritima - enzymology; Thermotoga maritima - genetics; transferases
• ISSN: 1399-0047; 0907-4449; 1399-0047
• DOI: 10.1107/S0907444900007708

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.