Small Angle Scattering Biological Data Bank SASBDB

Browse by MODEL: Hybrid

SASDEU5 – Adenylation domain of DNA ligase A

Sample:	DNA ligase A monomer, 38 kDa Mycobacterium tuberculosis protein
Buffer:	50 mM Tris-HCl, 200 mM NaCl, 2 mM β-mercaptoethanol, pH: 8
Experiment:	SAXS data collected at Anton Paar SAXSpace, CSIR-Central Drug Research Institute on 2018 Sep 27

Salt bridges at the subdomain interfaces of the adenylation domain and active-site residues of Mycobacterium tuberculosis NAD ⁺ -dependent DNA ligase A (MtbLigA) are important for the initial steps of nick-sealing activity Acta Crystallographica Section D Structural Biology 77(6) (2021)
Afsar M, Shukla A, Kumar N, Ramachandran R

R_g^Guinier	2.4	nm
D_max	8.8	nm
Volume^Porod	69	nm³

SASDJK3 – Native alpha-2-macroglobulin, glycosylated

Alpha-2-macroglobulin experimental SAS data

Sample:	Alpha-2-macroglobulin tetramer, 643 kDa Homo sapiens protein
Buffer:	20 mM HEPES, 150 mM NaCl, pH: 7.4
Experiment:	SAXS data collected at Bruker Nanostar w Excillum source, Department of Chemistry, iNANO building, Aarhus Uinversity on 2020 Jan 22

Structural Investigations of Human A2M Identify a Hollow Native Conformation That Underlies Its Distinctive Protease-Trapping Mechanism. Mol Cell Proteomics 20:100090 (2021)
Harwood SL, Lyngsø J, Zarantonello A, Kjøge K, Nielsen PK, Andersen GR, Pedersen JS, Enghild JJ

R_g^Guinier	7.7	nm
D_max	22.7	nm

SASDJL3 – Methylamine-treated alpha-2-macroglobulin, glycosylated

Sample:	Alpha-2-macroglobulin tetramer, 643 kDa Homo sapiens protein
Buffer:	20 mM HEPES, 150 mM NaCl, pH: 7.4
Experiment:	SAXS data collected at Bruker Nanostar w Excillum source, Department of Chemistry, iNANO building, Aarhus Uinversity on 2020 Jan 22

R_g^Guinier	6.7	nm
D_max	19.7	nm

SASDJM3 – Trypsin-treated alpha-2-macroglobulin, glycosylated

Cationic trypsinAlpha-2-macroglobulin experimental SAS data

Sample:	Cationic trypsin dimer, 52 kDa Bos taurus protein Alpha-2-macroglobulin tetramer, 643 kDa Homo sapiens protein
Buffer:	20 mM HEPES, 150 mM NaCl, pH: 7.4
Experiment:	SAXS data collected at Bruker Nanostar w Excillum source, Department of Chemistry, iNANO building, Aarhus Uinversity on 2020 Jan 15

R_g^Guinier	6.6	nm
D_max	19.7	nm

SASDJN3 – Native alpha-2-macroglobulin, deglycosylated

Sample:	Alpha-2-macroglobulin tetramer, 643 kDa Homo sapiens protein
Buffer:	20 mM HEPES, 150 mM NaCl, pH: 7.4
Experiment:	SAXS data collected at Bruker Nanostar w Excillum source, Department of Chemistry, iNANO building, Aarhus Uinversity on 2019 Apr 12

R_g^Guinier	7.6	nm
D_max	20.2	nm

SASDJP3 – Methylamine-treated alpha-2-macroglobulin, deglcycosylated

Sample:	Alpha-2-macroglobulin tetramer, 643 kDa Homo sapiens protein
Buffer:	20 mM HEPES, 150 mM NaCl, pH: 7.4
Experiment:	SAXS data collected at Bruker Nanostar w Excillum source, Department of Chemistry, iNANO building, Aarhus Uinversity on 2019 Apr 13

R_g^Guinier	6.6	nm
D_max	19.7	nm

SASDJQ3 – Trypsin-treated alpha-2-macroglobulin, deglycosylated

Sample:	Cationic trypsin dimer, 52 kDa Bos taurus protein Alpha-2-macroglobulin tetramer, 643 kDa Homo sapiens protein
Buffer:	20 mM HEPES, 150 mM NaCl, pH: 7.4
Experiment:	SAXS data collected at Bruker Nanostar w Excillum source, Department of Chemistry, iNANO building, Aarhus Uinversity on 2020 Jan 22

R_g^Guinier	6.6	nm
D_max	20.7	nm

SASDLJ3 – SH3 and multiple ankyrin repeat domains protein 3 (wild type)

SH3 and multiple ankyrin repeat domains protein 3 experimental SAS data

Sample:	SH3 and multiple ankyrin repeat domains protein 3 monomer, 88 kDa Rattus norvegicus protein
Buffer:	100mM NaH2PO4, 100mM NaCl, 0.5mM DTT,, pH: 6.5
Experiment:	SAXS data collected at EMBL P12, PETRA III on 2018 Jun 3

Autism associated SHANK3 missense point mutations impact conformational fluctuations and protein turnover at synapses. Elife 10 (2021)
Bucher M, Niebling S, Han Y, Molodenskiy D, Nia FH, Kreienkamp HJ, Svergun D, Kim E, Kostyukova AS, Kreutz MR, Mikhaylova M

R_g^Guinier	4.1	nm
D_max	14.0	nm
Volume^Porod	170	nm³

SASDLK3 – SH3 and multiple ankyrin repeat domains protein 3 with a point mutation (L68P)

Sample:	SH3 and multiple ankyrin repeat domains protein 3 monomer, 88 kDa Rattus norvegicus protein
Buffer:	100mM NaH2PO4, 100mM NaCl, 0.5mM DTT,, pH: 6.5
Experiment:	SAXS data collected at EMBL P12, PETRA III on 2018 Jun 3

R_g^Guinier	4.1	nm
D_max	14.8	nm
Volume^Porod	224	nm³

SASDLL3 – SH3 and multiple ankyrin repeat domains protein 3 with a point mutation (R12C)

Sample:	SH3 and multiple ankyrin repeat domains protein 3 monomer, 87 kDa Rattus norvegicus protein
Buffer:	100mM NaH2PO4, 100mM NaCl, 0.5mM DTT,, pH: 6.5
Experiment:	SAXS data collected at EMBL P12, PETRA III on 2018 Jun 3

R_g^Guinier	4.1	nm
D_max	13.8	nm
Volume^Porod	175	nm³

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