Crystallization of ClfA and ClfB fragments:: The fibrinogen-binding surface proteins of Staphylococcus aureus
Crystallization of ClfA and ClfB fragments:: The fibrinogen-binding surface proteins of Staphylococcus aureus
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DOI：
10.1107/s0907444998012426
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发表时间：
1999-02-01
期刊：
影响因子：
--
通讯作者：
Narayana, SVL
中科院分区：
文献类型：
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作者：
Deivanayagam, CCS;Perkins, S;Narayana, SVL
编码来自金黄色葡萄球菌的ClfA和ClfB的纤维蛋白原结合结构域的重组构建体已经结晶。ClfA晶体属正交晶系，空间群为P2（1）2（1）2（1），晶胞参数a = 39.58，B = 81.39，c = 112.65埃。完整的数据集被记录到2.1埃分辨率，并且具有2.3埃（3）Da（-1）的V-m，具有46.5%溶剂。表明每个不对称单元一个分子。ClfA与纤维蛋白原γ-链的17个氨基酸C-末端肽的共晶体衍射至2.1埃分辨率并具有晶胞参数a = 39.11，B = 81.39和c = 109.51埃，空间群为P2（1）2（1）2（1）Clf B以四面体空间群P4（1）2（1）2或P4（3）2（1）2，晶胞参数a = 96.31，B = 96.31和c = 84.13埃，衍射至2.45埃分辨率。在53%溶剂下的2.6埃（3）Da（-1）的估计V-m表明在不对称单元中有一个分子。
Recombinant constructs encoding the fibrinogen-binding domains of ClfA and ClfB from Staphylococcus aureus have been crystallized. ClfA was crystallized in the orthorhombic space group P2(1)2(1)2(1) with unit-cell parameters a = 39.58, b = 81.39 and c = 112.65 Angstrom. A complete data set was recorded to 2.1 Angstrom resolution and had a V-m of 2.3 Angstrom(3) Da(-1) with 46.5% solvent. suggesting one molecule per asymmetric unit. Co-crystals of ClfA with the 17 amino-acid C-terminal peptide of fibrinogen gamma-chain diffracted to 2.1 Angstrom resolution and had unit-cell parameters a = 39.11, b = 81.39 and c = 109.51 Angstrom in the space group P2(1)2(1)2(1) ClfB was crystallized in the tetragonal space group P4(1)2(1)2 or P4(3)2(1)2 with unit-cell parameters a = 96.31, b = 96.31 and c = 84.13 Angstrom and diffracted to 2.45 Angstrom resolution. The estimated V-m of 2.6 Angstrom(3) Da(-1) with 53% solvent indicated one molecule in the asymmetric unit.