Kalisz H M, Nogoceke E, Gommel D U, Hofmann B, Flohé L, Hecht H J
GBF - Gesellschaft für Biotechnologische Forschung, Mascheroder Weg 1, D-38124 Braunschweig, Germany.
Acta Crystallogr D Biol Crystallogr. 1999 Mar;55(Pt 3):696-8. doi: 10.1107/s0907444998015261.
The thioredoxin-related protein tryparedoxin I from Crithidia fasciculata has been crystallized using PEG 4000 as a precipitant. The enzyme forms long needle-shaped crystals which diffract to at least 1.7 A. A native data set has been collected at the DESY synchrotron from a flash-frozen crystal at 90 K to 1.7 A resolution. The data set shows that the crystals belong to the orthorhombic space group P212121 and have unit-cell parameters a = 37.94, b = 51. 39, c = 71.46 A. Tryparedoxin I is involved in a trypanothione-dependent peroxide metabolic pathway specific for trypanosomatids and may therefore be a suitable candidate for the design of drugs for the specific treatment of a variety of important tropical diseases caused by these parasites.
来自克氏锥虫的硫氧还蛋白相关蛋白锥虫硫氧还蛋白I已使用聚乙二醇4000作为沉淀剂进行了结晶。该酶形成长针状晶体，其衍射能力至少达到1.7埃。已在DESY同步加速器上从90K下的快速冷冻晶体收集了一个天然数据集，分辨率为1.7埃。数据集表明，这些晶体属于正交晶系空间群P212121，晶胞参数a = 37.94，b = 51.39，c = 71.46埃。锥虫硫氧还蛋白I参与了锥虫独有的依赖于三硫醇的过氧化物代谢途径，因此可能是设计用于特异性治疗由这些寄生虫引起的多种重要热带疾病的药物的合适候选物。
