Small Angle Scattering Biological Data Bank SASBDB

Browse by MACROMOLECULE type: protein

SASDE36 – Human ATP-citrate synthase (ACLY) in HBS

ATP-citrate synthase experimental SAS data

Sample:	ATP-citrate synthase tetramer, 458 kDa Homo sapiens protein
Buffer:	20mM HEPES, 150mM NaCl, pH: 7.2
Experiment:	SAXS data collected at EMBL P12, PETRA III on 2018 May 6

Structure of ATP citrate lyase and the origin of citrate synthase in the Krebs cycle. Nature 568(7753):571-575 (2019)
Verschueren KHG, Blanchet C, Felix J, Dansercoer A, De Vos D, Bloch Y, Van Beeumen J, Svergun D, Gutsche I, Savvides SN, Verstraete K

R_g^Guinier	6.0	nm
D_max	17.5	nm
Volume^Porod	738	nm³

SASDE46 – Human ATP-citrate synthers (ACLY) in HBS + Citrate

Sample:	ATP-citrate synthase tetramer, 458 kDa Homo sapiens protein
Buffer:	20mM HEPES, 150mM NaCl, 50mM Tris, 20mM citrate, pH: 7.2
Experiment:	SAXS data collected at EMBL P12, PETRA III on 2018 May 6

R_g^Guinier	6.1	nm
D_max	17.5	nm
Volume^Porod	747	nm³

SASDE56 – Human ATP-citrate synthase (ACLY) in HBS + Citrate + Coenzyme-A

Sample:	ATP-citrate synthase tetramer, 458 kDa Homo sapiens protein
Buffer:	20mM HEPES, 150mM NaCl, 50mM Tris, 20mM citrate, 2mM CoA, pH: 7.2
Experiment:	SAXS data collected at EMBL P12, PETRA III on 2018 May 5

R_g^Guinier	5.8	nm
D_max	16.5	nm
Volume^Porod	709	nm³

SASDE66 – C. limicola ATP-citrate lyase (ACL) in HBS

Sample:	ATP-citrate lyase tetramer, 429 kDa Chlorobium limicola protein
Buffer:	20mM HEPES, 150mM NaCl, pH: 7.2
Experiment:	SAXS data collected at EMBL P12, PETRA III on 2017 Sep 4

R_g^Guinier	6.1	nm
D_max	20.0	nm
Volume^Porod	666	nm³

SASDE76 – C. limicola ATP-citrate lyase (ACL) in HBS + Citrate

Sample:	ATP-citrate lyase tetramer, 429 kDa Chlorobium limicola protein
Buffer:	20mM HEPES, 150mM NaCl, 50mM Tris, 20mM citrate, pH: 7.2
Experiment:	SAXS data collected at EMBL P12, PETRA III on 2017 Sep 4

R_g^Guinier	6.0	nm
D_max	20.0	nm
Volume^Porod	672	nm³

SASDE86 – C. limicola ATP-citrate lyase (ACL) in HBS + Citrate + Coenzyme-A

Sample:	ATP-citrate lyase tetramer, 429 kDa Chlorobium limicola protein
Buffer:	20mM HEPES, 150mM NaCl, 50mM Tris, 20mM citrate, 2mM CoA, pH: 7.2
Experiment:	SAXS data collected at EMBL P12, PETRA III on 2017 Sep 4

R_g^Guinier	5.7	nm
D_max	17.5	nm
Volume^Porod	791	nm³

SASDFA3 – Human ATP-citrate synthase (ACLY) full length in HBS

Sample:	ATP-citrate synthase tetramer, 458 kDa Homo sapiens protein
Buffer:	20mM HEPES, 150mM NaCl, pH: 7.2
Experiment:	SAXS data collected at EMBL P12, PETRA III on 2017 Sep 4

R_g^Guinier	6.1	nm
D_max	19.0	nm
Volume^Porod	765	nm³

SASDFB3 – Human ATP-citrate synthers (ACLY) full length in HBS + Citrate

Sample:	ATP-citrate synthase tetramer, 458 kDa Homo sapiens protein
Buffer:	20mM HEPES, 150mM NaCl, 50mM Tris, 20mM citrate, pH: 7.2
Experiment:	SAXS data collected at EMBL P12, PETRA III on 2017 Sep 4

R_g^Guinier	6.2	nm
D_max	19.0	nm
Volume^Porod	787	nm³

SASDFC3 – Human ATP-citrate synthase (ACLY) full length in HBS + Citrate + Coenzyme-A

Sample:	ATP-citrate synthase tetramer, 458 kDa Homo sapiens protein
Buffer:	20mM HEPES, 150mM NaCl, 50mM Tris, 20mM citrate, 2mM CoA, pH: 7.2
Experiment:	SAXS data collected at EMBL P12, PETRA III on 2017 Sep 4

R_g^Guinier	5.9	nm
D_max	17.0	nm
Volume^Porod	775	nm³

SASDET6 – Polyglutamine-binding protein 1 p.Lys192Serfs7 (PQBP-1 XLID mutant K192Sfs7)

Polyglutamine-binding protein 1 p.Lys192Serfs*7 experimental SAS data

Polyglutamine-binding protein 1 p.Lys192Serfs*7 (PQBP-1 XLID mutant K192Sfs*7) Rg histogram

Sample:	Polyglutamine-binding protein 1 p.Lys192Serfs7 dimer, 47 kDa Homo sapiens* protein
Buffer:	Phosphate-buffered saline, pH: 7.4
Experiment:	SAXS data collected at EMBL X33, DORIS III, DESY on 2013 Feb 15

Frameshift PQBP-1 mutants K192S^fs*7 and R153S^fs*41 implicated in X-linked intellectual disability form stable dimers. J Struct Biol (2019)
Rahman SK, Okazawa H, Chen YW

R_g^Guinier	3.5	nm
D_max	13.0	nm
Volume^Porod	114	nm³

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