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

被引：4
|
作者：
Burke, J
Roujeinikova, A
Baker, PJ
Sedelnikova, S
Raasch, C
Liebl, W
Rice, DW [1 ]
机构：
[1] Univ Sheffield, Krebs Inst Biomolec Res, Dept Mol Biol & Biotechnol, Sheffield S10 2TN, S Yorkshire, England
[2] Univ Gottingen, Inst Mikrobiol & Genet, D-3400 Gottingen, Germany
来源：
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY | 2000年 / 56卷
关键词：
D O I：
10.1107/S0907444900007708
中图分类号：
Q5 [生物化学];
学科分类号：
071010 ; 081704 ;
摘要：
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 Angstrom. The asymmetric unit appears to contain one subunit, corresponding to a very low packing density of 4.0 Angstrom(3) Da(-1). The crystals diffract X-rays to at least 2.4 Angstrom resolution on a synchrotron-radiation source.
引用
收藏
页码：1049 / 1050
页数：2
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