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Expression, purification, crystallization and preliminary crystallographic analysis of a putative Clostridium difficile surface protein Cwp19.

作者信息

Kirby Jonathan M, Thiyagarajan Nethaji, Roberts April K, Shone Clifford C, Acharya K Ravi

机构信息

Department of Biology and Biochemistry, University of Bath, Claverton Down, Bath BA2 7AY, England.

出版信息

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Jul 1;67(Pt 7):762-7. doi: 10.1107/S1744309111016770. Epub 2011 Jun 30.

DOI:10.1107/S1744309111016770
PMID:21795789
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC3144791/
Abstract

Cwp19 is a putatively surface-located protein from Clostridium difficile. A recombinant N-terminal protein (residues 27-401) lacking the signal peptide and the C-terminal cell-wall-binding repeats (PFam04122) was crystallized using the sitting-drop vapour-diffusion method and diffracted to 2 Å resolution. The crystal appeared to belong to the primitive monoclinic space group P2(1), with unit-cell parameters a=109.1, b=61.2, c=109.2 Å, β=111.85°, and is estimated to contain two molecules of Cwp19 per asymmetric unit.

摘要
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9522/3144791/ee0272345561/f-67-00762-fig7.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9522/3144791/9297503b3020/f-67-00762-fig1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9522/3144791/05aa700f8380/f-67-00762-fig2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9522/3144791/dd0ae369130d/f-67-00762-fig3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9522/3144791/cccd90d56dfd/f-67-00762-fig4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9522/3144791/aebcc397bc25/f-67-00762-fig5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9522/3144791/831b8dd0e1c0/f-67-00762-fig6.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9522/3144791/ee0272345561/f-67-00762-fig7.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9522/3144791/9297503b3020/f-67-00762-fig1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9522/3144791/05aa700f8380/f-67-00762-fig2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9522/3144791/dd0ae369130d/f-67-00762-fig3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9522/3144791/cccd90d56dfd/f-67-00762-fig4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9522/3144791/aebcc397bc25/f-67-00762-fig5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9522/3144791/831b8dd0e1c0/f-67-00762-fig6.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9522/3144791/ee0272345561/f-67-00762-fig7.jpg

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J Med Microbiol. 2011 Aug;60(Pt 8):1225-1228. doi: 10.1099/jmm.0.028472-0. Epub 2011 Jan 20.
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Clostridium difficile: progress and challenges.艰难梭菌:进展与挑战。
Ann N Y Acad Sci. 2010 Dec;1213:62-9. doi: 10.1111/j.1749-6632.2010.05863.x.
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Structure of human stabilin-1 interacting chitinase-like protein (SI-CLP) reveals a saccharide-binding cleft with lower sugar-binding selectivity.人稳定素-1 相互作用几丁质样蛋白(SI-CLP)的结构揭示了一个具有较低糖结合选择性的糖结合裂隙。
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Structural organization of the functional domains of Clostridium difficile toxins A and B.艰难梭菌毒素 A 和 B 的功能域的结构组织。
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