Alexopoulos Eftichia, Kanjee Usheer, Snider Jamie, Houry Walid A, Pai Emil F
Department of Biochemistry, University of Toronto, 1 King's College Circle, Medical Sciences Building, Toronto, Ontario M5S1A8, Canada.
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 Aug 1;64(Pt 8):700-6. doi: 10.1107/S1744309108018757. Epub 2008 Jul 5.
The decameric inducible lysine decarboxylase (LdcI) from Escherichia coli has been crystallized in space groups C2 and C222(1); the Ta6Br12(2+) cluster was used to derivatize the C2 crystals. The method of single isomorphous replacement with anomalous scattering (SIRAS) as implemented in SHELXD was used to solve the Ta6Br12(2+)-derivatized structure to 5 A resolution. Many of the Ta6Br12(2+)-binding sites had twofold and fivefold noncrystallographic symmetry. Taking advantage of this feature, phase modification was performed in DM. The electron-density map of LdcI displays many features in agreement with the low-resolution negative-stain electron-density map [Snider et al. (2006), J. Biol. Chem. 281, 1532-1546].
来自大肠杆菌的十聚体诱导型赖氨酸脱羧酶(LdcI)已在空间群C2和C222(1)中结晶;Ta6Br12(2+)簇用于衍生化C2晶体。使用SHELXD中实现的单同晶置换加反常散射(SIRAS)方法将Ta6Br12(2+)衍生化结构解析到5 Å分辨率。许多Ta6Br12(2+)结合位点具有二次和五次非晶体学对称性。利用这一特性,在DM中进行了相位修正。LdcI的电子密度图显示出许多与低分辨率负染电子密度图一致的特征[Snider等人(2006年),《生物化学杂志》281,1532 - 1546]。