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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Crystallization and preliminary crystallographic analysis of a novel haemolytic lectin from the mushroom Laetiporus sulphureus.
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Crystallization and preliminary crystallographic analysis of a novel haemolytic lectin from the mushroom Laetiporus sulphureus.

机译:结晶和初步的晶体分析小说溶血性凝集素的

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The novel haemolytic lectin from the parasitic mushroom Laetiporus sulphureus (LSL) is a homotetramer ( approximately 140 kDa) composed of subunits associated by non-covalent bonds. It exhibits haemagglutination and haemolytic activities, both of which are inhibited by N-acetyllactosamine. The structural similarity found between LSL and the bacterial pore-forming toxins mosquitocidal toxin (MTX2) from Bacillus sphaericus and alpha-toxin from Clostridium septicum points to a mechanism of biological action involving the formation of pores in the target membranes. LSL has been crystallized using the hanging-drop vapour-diffusion method at 291 K. Diffraction-quality hexagonal crystals have unit-cell parameters a = b = 101.8, c = 193.9 A and belong to space group P6(3)22. A 2.7 A native data set was collected with an R(merge) of 9.2%.
机译:这部小说溶血性寄生凝集素蘑菇Laetiporus sulphureus (LSL)homotetramer(大约140 kDa)组成的子单元通过非共价债券有关。展览血细胞凝集和溶血性活动,所抑制N-acetyllactosamine。发现LSL和细菌造孔之间从芽孢杆菌毒素mosquitocidal毒素(MTX2)sphaericus和alpha-toxin梭状芽孢杆菌坏疽毒素的生物机制行动涉及的毛孔的形成目标膜。在291的悬滴vapour-diffusion方法k . Diffraction-quality六角晶体晶胞参数a = b = 101.8, c = 193.9和属于空间群P6(3) 22。数据集收集R(合并)的9.2%。

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