Bioisis

"TIA-RRM123, Mut1- Y10A, F50A (CHESS)"

Experimental SAS Curve

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Low_res_thumbnail

Experimental Mass

30,000 Da

Experimental Details for BID:  2TM1KP
Experiment ID: 71
Collected at: CHESS BL F2
Contributors: Bauer, W.J. ,  Heath, J. ,  Jenkins, J.L. ,  Kielkopf, C.L.
Pro-Apoptotic, alternative splicing factor TIA-1 RRM1-RRM2-RRM3 domains in the absence of RNA, for comparison with TIA-1/RNA complex. The average solution conformation of three TIA-1 RRMs is an obtuse V shape. The mutations to RRM1 (Y10A and F50A) had no detectable effect on the relative positioning of the three RRM domains, the Rg, Dmax dimensions, Kratky plot or the P(r) function.
Extrapolated to zero concentration from 4 different concentrations between 1 and 10 mg/mL

Electron Pair Distribution

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       Dmax → 100 Å


Guinier Plot

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     Guinier Rg → 29.6 Å

Real Space Rg → 30.8 Å

The Guinier plot is used to estimate the radius of gyration, Rg, which is taken from the slope of a line observed at low scattering angles (typically in the range where q* Rg < 1.3). This should be in reasonable agreement with the real space Rg.


Kratky Plot

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The Kratky plot can be used to visually assess the degree of "unfoldedness" of a protein or RNA sample. The plot of a well-behaved folded protein approaches the baseline at high q values creating a parabolic shape.


DAMMIN/F Model

DAMMIN/F result was determined with the following:

Space GroupP1
NSD | RMSD0.72 
variance(NSD | RMSD)0.03 
Number of Models in Average10 

Additional Experimental Details
Title

TIA-RRM123, Mut1- Y10A, F50A (CHESS)

Description

Pro-Apoptotic, alternative splicing factor TIA-1 RRM1-RRM2-RRM3 domains in the absence of RNA, for comparison with TIA-1/RNA complex. The average solution conformation of three TIA-1 RRMs is an obtuse V shape. The mutations to RRM1 (Y10A and F50A) had no detectable effect on the relative positioning of the three RRM domains, the Rg, Dmax dimensions, Kratky plot or the P(r) function.

Publication

Three RNA Recognition Motifs Participate in RNA Recognition and Structural Organization by the Pro-Apoptotic Factor TIA-1, Journal of Molecular Biology xx (2011) xxx–xxx

Contributors

Bauer, W.J. ,  Heath, J. ,  Jenkins, J.L. ,  Kielkopf, C.L.

Genomics and Proteomics

The experiment is composed of a single gene/ORF

Abbreviated name: TIA123Mut1

Annotation: TIA-1 RRM1-RRM2-RRM3 residues 1-274 with two mutations to RRM1, Y10A and F50A.

GPLGSMEDEM PKTLYVGNLS RDVTEALILQ LFSQIGPCKN CKMIMDTAGN DPYCFVEFHE HRHAAAALAA MNGRKIMGKE VKVNWATTPS SQKKDTSNHF HVFVGDLSPE ITTEDIKAAF APFGRISDAR VVKDMATGKS KGYGFVSFFN KWDAENAIQQ MGGQWLGGRQ IRTNWATRKP PAPKSTYESN TKQLSYDEVV NQSSPSNCTV YCGGVTSGLT EQLMRQTFSP FGQIMEIRVF PDKGYSFVRF NSHESAAHAI VSVNGTTIEG HVVKCYWGK
categoryamino acid composition(%)
HydrophobicI(4.7) V(7.2) L(4.3) M(3.6) A(7.5) G(8.6) P(4.7)
AromaticF(5.4) W(1.8) Y(2.9)
HydrophilicR(3.9) K(6.8) E(5.4) D(4.3) Q(4.3) N(5.0) H(2.9) S(7.9) T(6.8) C(2.2)