Cloning, expression, crystallization and preliminary X-ray analysis of the DNA-binding protein Sso10a from Sulfolobus solfataricus.
Cloning, expression, crystallization and preliminary X-ray analysis of the DNA-binding protein Sso10a from Sulfolobus solfataricus.
复制标题
硫磺硫化叶菌 DNA 结合蛋白 Sso10a 的克隆、表达、结晶和初步 X 射线分析。
DOI：
10.1107/s090744490301062x
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发表时间：
2003
期刊：
影响因子：
--
通讯作者：
Meehan,E
中科院分区：
文献类型：
--
作者：
Teale,MJ;Kahsai,M;Singh,SK;Edmondson,SP;Gupta,R;Shriver,JW;Meehan,E
The gene for the DNA-binding protein Sso10a from the hyperthermophilic archaeon Sulfolobus solfataricus was cloned and overexpressed in Escherichia coli. Crystals of the purified protein have been grown that diffract to beyond 2.15 Å resolution. The protein crystals belong to the orthorhombic space group P212121, with unit-cell parameters a = 57.24, b = 60.16, c = 69.96 Å. With one dimer per asymmetric unit, the crystal to volume per protein mass (VM) is 2.9 Å3 Da−1 and the solvent content is ∼57%. Complete X-ray diffraction native data were collected from a single crystal and processed to 2.15 Å.
