Chen Chun-Jung, Liu Ming-Yih, Chen Yi-Ting, LeGall Jean
X-ray Structural Biology Group, National Synchrotron Radiation Research Center, Hsinchu 30077, Taiwan.
Biochem Biophys Res Commun. 2003 Sep 5;308(4):684-8. doi: 10.1016/s0006-291x(03)01463-3.
Rubredoxin (D.g. Rd), a small non-heme iron-sulfur protein shown to function as a redox coupling protein from the sulfate reducing bacteria Desulfovibrio gigas, has been crystallized using the hanging-drop vapor diffusion method and macroseeding method. Rubredoxin crystals diffract to an ultra-high resolution 0.68 A using synchrotron radiation X-ray, and belong to the space group P2(1) with unit-cell parameters a=19.44 A, b=41.24 A, c=24.10 A, and beta=108.46 degrees. The data set of single-wavelength anomalous dispersion signal of iron in the native crystal was also collected for ab initio structure re-determination. Preliminary analysis indicates that there is one monomer with a [Fe-4S] cluster in each asymmetric unit. The crystal structure at this ultra-high resolution will reveal the details of its biological function. The crystal character and data collection strategy for ultra-high resolution will also be discussed.
红氧还蛋白（脱硫弧菌红氧还蛋白，D.g. Rd）是一种小型非血红素铁硫蛋白，已被证明是来自脱硫弧菌的氧化还原偶联蛋白，采用悬滴气相扩散法和宏观接种法进行了结晶。利用同步辐射X射线，红氧还蛋白晶体的衍射分辨率高达0.68 Å，属于空间群P2(1)，晶胞参数为a = 19.44 Å，b = 41.24 Å，c = 24.10 Å，β = 108.46°。还收集了天然晶体中铁的单波长反常色散信号数据集，用于从头结构重新测定。初步分析表明，每个不对称单元中有一个含有[Fe-4S]簇的单体。这种超高分辨率的晶体结构将揭示其生物学功能的细节。还将讨论超高分辨率的晶体特性和数据收集策略。
