Small Angle Scattering Biological Data Bank SASBDB

SASBDB entries for UniProt ID:

SASDGK2 – Interleukin 11/Interleukin 11 receptor alpha complex

UniProt ID: Q14626 (23-319) Interleukin-11 receptor subunit alpha

UniProt ID: A8K3F7 (32-199) Interleukin 11

Interleukin-11 receptor subunit alphaInterleukin 11 experimental SAS data

Sample:	Interleukin-11 receptor subunit alpha monomer, 32 kDa Homo sapiens protein Interleukin 11 monomer, 18 kDa Homo sapiens protein
Buffer:	20 mM Tris, 150 mM NaCl, 0.2% sodium azide, pH: 8.5
Experiment:	SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2019 Jun 8

The structure of the extracellular domains of human interleukin 11 α-receptor reveals mechanisms of cytokine engagement Journal of Biological Chemistry :jbc.RA119.012351 (2020)
Metcalfe R, Aizel K, Zlatic C, Nguyen P, Morton C, Lio D, Cheng H, Dobson R, Parker M, Gooley P, Putoczki T, Griffin M

R_g^Guinier	3.3	nm
D_max	10.2	nm
Volume^Porod	84	nm³

SASDGL2 – Ring opening PaaZ from the phenylacetate degradation pathway (E. coli K12)

UniProt ID: P77455 (1-681) Bifunctional protein PaaZ

Bifunctional protein PaaZ experimental SAS data

Sample:	Bifunctional protein PaaZ hexamer, 438 kDa Escherichia coli protein
Buffer:	25 mM HEPES, 50 mM NaCl, pH: 7.4
Experiment:	SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2015 Feb 24

Molecular basis for metabolite channeling in a ring opening enzyme of the phenylacetate degradation pathway. Nat Commun 10(1):4127 (2019)
Sathyanarayanan N, Cannone G, Gakhar L, Katagihallimath N, Sowdhamini R, Ramaswamy S, Vinothkumar KR

R_g^Guinier	6.2	nm
D_max	20.0	nm
Volume^Porod	636	nm³

SASDGM2 – R16-24 del44-54 human dystrophin fragment

UniProt ID: P11532 (1990-3040) Human dystrophin central domain R16-24 del44-54 fragment

Human dystrophin central domain R16-24 del44-54 fragment experimental SAS data

Human dystrophin central domain R16-24 del44-54 fragment Kratky plot

Sample:	Human dystrophin central domain R16-24 del44-54 fragment monomer, 57 kDa Homo sapiens protein
Buffer:	20 mM Na-phosphate, 300 mM NaCl, 1 mM EDTA, 2% glycerol,, pH: 7.5
Experiment:	SAXS data collected at SWING, SOLEIL on 2019 Jul 8

Dystrophin SAXS data
Raphael Dos Santos Morais

R_g^Guinier	6.4	nm
D_max	25.0	nm
Volume^Porod	159	nm³

SASDGP2 – Thymine dioxygenase full length J-DNA binding protein (JBP1)

UniProt ID: Q9U6M1 (2-827) Thymine dioxygenase JBP1

Thymine dioxygenase JBP1 experimental SAS data

Sample:	Thymine dioxygenase JBP1 monomer, 93 kDa Leishmania tarentolae protein
Buffer:	20 mM HEPES, 200 mM NaCl, 1 mM TCEP, pH: 7.5
Experiment:	SAXS data collected at BM29, ESRF on 2016 Feb 21

The domain architecture of protozoan protein J-DNA-binding protein 1 suggests synergy between base J DNA binding and thymidine hydroxylase activity. J Biol Chem (2019)
Adamopoulos A, Heidebrecht T, Roosendaal J, Touw WG, Phan IQ, Beijnen J, Perrakis A

R_g^Guinier	3.4	nm
D_max	12.0	nm
Volume^Porod	128	nm³

SASDGQ2 – Thymine dioxygenase lacking the JDNA binding domain Delta-JDBD (Δ-JDBD)

UniProt ID: Q9U6M1 (2-827) Delta-JDBD

Sample:	Delta-JDBD monomer, 72 kDa Leismania tarentolae protein
Buffer:	20 mM HEPES, 200 mM NaCl, 1 mM TCEP, pH: 7.5
Experiment:	SAXS data collected at BM29, ESRF on 2016 Feb 21

R_g^Guinier	3.1	nm
D_max	9.9	nm
Volume^Porod	108	nm³

SASDGR2 – Thymine dioxygenase J-containing DNA binding domain (JDBD)

UniProt ID: Q9U6M1 (382-561) J-DNA binding domain

J-DNA binding domain experimental SAS data

Sample:	J-DNA binding domain monomer, 21 kDa Leishmania tarentolae protein
Buffer:	20 mM HEPES, 200 mM NaCl, 1 mM TCEP, pH: 7.5
Experiment:	SAXS data collected at BM29, ESRF on 2017 Feb 4

R_g^Guinier	2.2	nm
D_max	7.1	nm
Volume^Porod	38	nm³

SASDGT2 – Thymine dioxygenase J-containing DNA binding domain in complex with J-23-DNA (JDBD:J-23-DNA)

UniProt ID: Q9U6M1 (382-561) J-DNA binding domain

UniProt ID: None (None-None) J-DNA (23mer)

J-DNA binding domainJ-DNA (23mer) experimental SAS data

J-DNA binding domain J-DNA (23mer) Kratky plot

Sample:	J-DNA binding domain monomer, 21 kDa Leishmania tarentolae protein J-DNA (23mer) monomer, 14 kDa DNA
Buffer:	20 mM HEPES, 200 mM NaCl, 1 mM TCEP, pH: 7.5
Experiment:	SAXS data collected at BM29, ESRF on 2016 Feb 21

R_g^Guinier	2.5	nm
D_max	8.6	nm
Volume^Porod	43	nm³

SASDGU2 – Thymine dioxygenase full length J-DNA binding protein in complex with J-23-DNA (JBP1:J-23-DNA)

UniProt ID: Q9U6M1 (2-827) Thymine dioxygenase JBP1

UniProt ID: None (None-None) J-DNA (23mer)

Thymine dioxygenase JBP1J-DNA (23mer) experimental SAS data

Thymine dioxygenase JBP1 J-DNA (23mer) Kratky plot

Sample:	Thymine dioxygenase JBP1 monomer, 93 kDa Leishmania tarentolae protein J-DNA (23mer) monomer, 14 kDa DNA
Buffer:	20 mM HEPES, 200 mM NaCl, 1 mM TCEP, pH: 7.5
Experiment:	SAXS data collected at BM29, ESRF on 2016 Feb 21

R_g^Guinier	4.1	nm
D_max	14.1	nm
Volume^Porod	148	nm³

SASDGV2 – The Pyrococcus furiosus Box C/D sRNP complex reconstituted with 1H Nop5, 1H L7Ae, 1H st-sR26 RNA, 1H substrate D' and 2H Fibrillarin (SANS data in 42% v/v D2O)

UniProt ID: Q8U4M2 (1-227) Fibrillarin-like rRNA/tRNA 2'-O-methyltransferase

UniProt ID: Q8U160 (1-123) 50S ribosomal protein L7Ae

UniProt ID: Q8U4M1 (1-402) NOP5/NOP56 related protein

UniProt ID: None (None-None) pyrococcus furiosus sR26 stabilized construct

UniProt ID: None (None-None) Pyrococcus furiosus sR26 substrate D'

Fibrillarin-like rRNA/tRNA 2'-O-methyltransferase50S ribosomal protein L7AeNOP5/NOP56 related proteinpyrococcus furiosus sR26 stabilized constructPyrococcus furiosus sR26 substrate D' experimental SAS data

Sample:	Fibrillarin-like rRNA/tRNA 2'-O-methyltransferase dimer, 52 kDa Pyrococcus furiosus protein 50S ribosomal protein L7Ae dimer, 27 kDa Pyrococcus furiosus protein NOP5/NOP56 related protein dimer, 94 kDa Pyrococcus furiosus protein Pyrococcus furiosus sR26 stabilized construct monomer, 24 kDa Pyrococcus furiosus RNA Pyrococcus furiosus sR26 substrate D' monomer, 4 kDa Pyrococcus furiosus RNA
Buffer:	50 mM phosphate 500 mM NaCl 42%D2O, pH: 6.6
Experiment:	SANS data collected at KWS1, FRM2 on 2015 May 24

The guide sRNA sequence determines the activity level of box C/D RNPs. Elife 9 (2020)
Graziadei A, Gabel F, Kirkpatrick J, Carlomagno T

R_g^Guinier	4.9	nm
D_max	16.0	nm
Volume^Porod	87	nm³

SASDGW2 – The Pyrococcus furiosus Box C/D sRNP complex reconstituted with 1H Fibrillarin, 1H L7Ae, 1H st-sR26 RNA, 1H substrate D' and 2H Nop5 (SANS data in 42% v/v D2O)