Crystallization and preliminary X-ray crystallographic studies on maltosyltransferase from Thermotoga maritima.
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 P4(1)22 or its enantiomorph P4(3)22, with unit-cell parameters a = b = 148.7, c = 106.7 A. The asymmetric unit appears to contain one subunit, corresponding to a very low packing density of 4.0 A(3) Da(-1). The crystals diffract X-rays to at least 2.4 A resolution on a synchrotron-radiation source.
Burke
J
J
Krebs Institute for Biomolecular Research, Department of Molecular Biology and Biotechnology, The University of Sheffield, Sheffield S10 2TN, England.
Roujeinikova
A
A
Baker
P J
PJ
Sedelnikova
S
S
Raasch
C
C
Liebl
W
W
Rice
D W
DW
D003460:Crystallization; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000235:genetics; D006004:Glycogen Debranching Enzyme System / Q000737:chemistry* / Q000235:genetics; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics; D020124:Thermotoga maritima / Q000201:enzymology* / Q000235:genetics
D006004:Glycogen Debranching Enzyme System; D011994:Recombinant Proteins; C020569:4 alpha-glucanotransferase