Kwon Soo Young, Kang Beom Sik, Kim Myung Hee, Kim Kyung Jin
Beamline Division, Pohang Accelerator Laboratory, Pohang, Kyungbuk 790-784, Republic of Korea.
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Dec 1;63(Pt 12):1058-60. doi: 10.1107/S1744309107056953. Epub 2007 Nov 30.
Structural maintenance of chromosome (SMC) proteins play diverse roles in cellular DNA reassembly by directly interacting with DNA. They require non-SMC proteins for their proper function; these include the conserved segregation and condensation proteins (Scps) in prokaryotes. ScpB from Mycobacterium tuberculosis was crystallized using the sitting-drop vapour-diffusion method in the presence of 2 M NaCl and 10% PEG 6000 at 295 K. X-ray diffraction data were collected to a maximum resolution of 2.3 A at a synchrotron beamline. The crystal belongs to the hexagonal space group R32, with unit-cell parameters a = b = 136.69, c = 78.55 A, gamma = 120 degrees . With one molecule per asymmetric unit, the crystal volume per unit protein weight (V(M)) is 2.95 A(3) Da(-1). The structure was solved by the single anomalous dispersion method and structure refinement is in progress.
染色体结构维持（SMC）蛋白通过与DNA直接相互作用，在细胞DNA重新组装过程中发挥多种作用。它们需要非SMC蛋白来实现其正常功能；这些非SMC蛋白包括原核生物中保守的分离和凝聚蛋白（Scps）。结核分枝杆菌的ScpB在295 K下，于2 M NaCl和10% PEG 6000存在的条件下，采用坐滴气相扩散法进行结晶。在同步加速器光束线上收集到最大分辨率为2.3 Å的X射线衍射数据。该晶体属于六方空间群R32，晶胞参数a = b = 136.69，c = 78.55 Å，γ = 120°。每个不对称单元中有一个分子，单位蛋白重量的晶体体积（V(M)）为2.95 ų Da⁻¹。该结构通过单波长反常散射法解析，结构精修正在进行中。
