Crystallization and preliminary X-ray crystallographic analysis of the variable domain of Scl2.3, a streptococcal collagen-like protein from invasive M3-type Streptococcus pyogenes.
Crystallization and preliminary X-ray crystallographic analysis of the variable domain of Scl2.3, a streptococcal collagen-like protein from invasive M3-type Streptococcus pyogenes.
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Scl2.3 可变结构域的结晶和初步 X 射线晶体学分析，Scl2.3 是一种来自侵袭性 M3 型化脓性链球菌的链球菌胶原蛋白样蛋白。
DOI：
10.1107/s174430911302068x
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发表时间：
2013
期刊：
影响因子：
--
通讯作者：
Berisio,Rita
中科院分区：
文献类型：
--
作者：
Squeglia,Flavia;Bachert,Beth;Romano,Maria;Lukomski,Slawomir;Berisio,Rita
Streptococcal collagen-like proteins (Scls) are widely expressed by the well recognized human pathogen Streptococcus pyogenes. These surface proteins contain a signature central collagen-like region and an amino-terminal globular domain, termed the variable domain, which is protruded away from the cell surface by the collagen-like domain. Despite their recognized importance in bacterial pathogenicity, no structural information is presently available on proteins of the Scl class. The variable domain of Scl2 from invasive M3-type S. pyogenes has successfully been crystallized using vapour-diffusion methods. The crystals diffracted to 1.5 Å resolution and belonged to space group H32, with unit-cell parameters a = 44.23, b = 44.23, c = 227.83 Å. The crystal structure was solved by single-wavelength anomalous dispersion using anomalous signal from a europium chloride derivative.|
