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231224s2013 xx |||||o 00| ||eng c |
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7 |
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|a 10.1107/S0909049513022164
|2 doi
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|a pubmed24n0772.xml
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|a (DE-627)NLM231658451
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|a (NLM)24121347
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|a DE-627
|b ger
|c DE-627
|e rakwb
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| 041 |
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|a eng
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| 100 |
1 |
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|a Adachi, Motoyasu
|e verfasserin
|4 aut
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| 245 |
1 |
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|a Creation and structure determination of an artificial protein with three complete sequence repeats
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| 264 |
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1 |
|c 2013
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| 336 |
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|a Text
|b txt
|2 rdacontent
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| 337 |
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|a ƒaComputermedien
|b c
|2 rdamedia
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| 338 |
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|a ƒa Online-Ressource
|b cr
|2 rdacarrier
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| 500 |
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|a Date Completed 22.05.2014
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| 500 |
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|a Date Revised 21.10.2021
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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|a Symfoil-4P is a de novo protein exhibiting the threefold symmetrical β-trefoil fold designed based on the human acidic fibroblast growth factor. First three asparagine-glycine sequences of Symfoil-4P are replaced with glutamine-glycine (Symfoil-QG) or serine-glycine (Symfoil-SG) sequences protecting from deamidation, and His-Symfoil-II was prepared by introducing a protease digestion site into Symfoil-QG so that Symfoil-II has three complete repeats after removal of the N-terminal histidine tag. The Symfoil-QG and SG and His-Symfoil-II proteins were expressed in Eschericha coli as soluble protein, and purified by nickel affinity chromatography. Symfoil-II was further purified by anion-exchange chromatography after removing the HisTag by proteolysis. Both Symfoil-QG and Symfoil-II were crystallized in 0.1 M Tris-HCl buffer (pH 7.0) containing 1.8 M ammonium sulfate as precipitant at 293 K; several crystal forms were observed for Symfoil-QG and II. The maximum diffraction of Symfoil-QG and II crystals were 1.5 and 1.1 Å resolution, respectively. The Symfoil-II without histidine tag diffracted better than Symfoil-QG with N-terminal histidine tag. Although the crystal packing of Symfoil-II is slightly different from Symfoil-QG and other crystals of Symfoil derivatives having the N-terminal histidine tag, the refined crystal structure of Symfoil-II showed pseudo-threefold symmetry as expected from other Symfoils. Since the removal of the unstructured N-terminal histidine tag did not affect the threefold structure of Symfoil, the improvement of diffraction quality of Symfoil-II may be caused by molecular characteristics of Symfoil-II such as molecular stability
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|a Journal Article
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| 650 |
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|a Symfoil
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| 650 |
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4 |
|a acidic FGF
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| 650 |
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4 |
|a protein design
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| 650 |
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7 |
|a Proteins
|2 NLM
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| 700 |
1 |
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|a Shimizu, Rumi
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Kuroki, Ryota
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Blaber, Michael
|e verfasserin
|4 aut
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| 773 |
0 |
8 |
|i Enthalten in
|t Journal of synchrotron radiation
|d 1994
|g 20(2013), Pt 6 vom: 07. Nov., Seite 953-7
|w (DE-627)NLM09824129X
|x 1600-5775
|7 nnns
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| 773 |
1 |
8 |
|g volume:20
|g year:2013
|g number:Pt 6
|g day:07
|g month:11
|g pages:953-7
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| 856 |
4 |
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|u http://dx.doi.org/10.1107/S0909049513022164
|3 Volltext
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|a GBV_USEFLAG_A
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|a SYSFLAG_A
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|a GBV_NLM
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|a GBV_ILN_40
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| 912 |
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|a GBV_ILN_350
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| 912 |
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|a GBV_ILN_2005
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| 951 |
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|a AR
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| 952 |
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|d 20
|j 2013
|e Pt 6
|b 07
|c 11
|h 953-7
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