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Purification, nanocrystallization and preliminary X-ray analysis of a C-terminal part of tropomodulin protein 1, isoform A, from Caenorhabditis elegans.

作者信息

Ding Haitao, Qiu Shihong, Bunzel Robert J, Luo Danlin, Arabashi Alireza, Lu Shanyun, Symersky Jindrich, Nagy Lisa A, DeLucas Lawrence J, Li Songlin, Luo Ming

机构信息

Life Sciences College, Peking University, Beijing 100871, People's Republic of China.

出版信息

Acta Crystallogr D Biol Crystallogr. 2003 Jun;59(Pt 6):1106-8. doi: 10.1107/s0907444903008217. Epub 2003 May 23.

DOI:10.1107/s0907444903008217
PMID:12777789
Abstract

The C-terminal part of tropomodulin protein 1, isoform A, from Caenorhabditis elegans was expressed in Escherichia coli and purified to homogeneity. Optimized from the initial nanoscreen, crystals grew to dimensions of 0.25 x 0.15 x 0.15 mm at 277 K using 28.0%(v/v) PEG 400 as the precipitant by the hanging-drop vapor-diffusion technique. A data set of 94.9% completeness was collected to a resolution of 1.98 A at 100 K using a synchrotron X-ray source (SER-CAT). The crystals belong to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 31.7, b = 50.6, c = 107.1 A, and contained one molecule per asymmetric unit.

摘要

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