Small Angle Scattering Biological Data Bank SASBDB

SASDFF5 – Protein DPCD

Sample:	Protein DPCD monomer, 24 kDa Homo sapiens protein
Buffer:	20 mM HEPES, 150 mM NaCl, 1% glycerol, 5 mM TCEP, pH: 7.5
Experiment:	SAXS data collected at SWING, SOLEIL on 2019 Mar 21

Deciphering cellular and molecular determinants of human DPCD protein in complex with RUVBL1/RUVBL2 AAA-ATPases. J Mol Biol :167760 (2022)
Dos Santos Morais R, Santo PE, Ley M, Schelcher C, Abel Y, Plassart L, Deslignière E, Chagot ME, Quinternet M, Paiva ACF, Hessmann S, Morellet N, M F Sousa P, Vandermoere F, Bertrand E, Charpentier B,...

R_g^Guinier	2.2	nm
D_max	12.3	nm
Volume^Porod	39	nm³

SASDFG5 – His-RuvBl1/RuvBl2 dodecamer

RuvB-like 1RuvB-like 2 experimental SAS data

Sample:	RuvB-like 1 hexamer, 311 kDa Homo sapiens protein RuvB-like 2 hexamer, 311 kDa Homo sapiens protein
Buffer:	20 mM HEPES, 150 mM NaCl, 1% glycerol, 5 mM TCEP, pH: 7.5
Experiment:	SAXS data collected at SWING, SOLEIL on 2019 Mar 21

R_g^Guinier	6.2	nm
D_max	20.0	nm
Volume^Porod	1490	nm³

SASDFH5 – DPCD His-RuvBl1/RuvBl2 hexamer complex

Protein DPCDRuvB-like 1RuvB-like 2 experimental SAS data

Sample:	Protein DPCD trimer, 71 kDa Homo sapiens protein RuvB-like 1 trimer, 155 kDa Homo sapiens protein RuvB-like 2 trimer, 156 kDa Homo sapiens protein
Buffer:	20 mM HEPES, 150 mM NaCl, 1% glycerol, 5 mM TCEP, pH: 7.5
Experiment:	SAXS data collected at SWING, SOLEIL on 2019 Mar 21

R_g^Guinier	5.4	nm
D_max	15.9	nm
Volume^Porod	856	nm³

SASDNU5 – Lysin from Streptococcus phage P7951 ∆1-208

lysin [Streptococcus phage P7951] experimental SAS data

Sample:	lysin [Streptococcus phage P7951] hexamer, 65 kDa Streptococcus phage P7951 protein
Buffer:	50 mM HEPES, 500 mM NaCl, and 1% glycerol, pH: 7
Experiment:	SAXS data collected at BM29, ESRF on 2021 Nov 21

On the Occurrence and Multimerization of Two-Polypeptide Phage Endolysins Encoded in Single Genes. Microbiol Spectr :e0103722 (2022)
Pinto D, Gonçalo R, Louro M, Silva MS, Hernandez G, Cordeiro TN, Cordeiro C, São-José C

R_g^Guinier	3.1	nm
D_max	10.1	nm
Volume^Porod	111	nm³

SASDLZ9 – Streptococcus pneumoniae lipid II isoglutaminyl synthase MurT:GatD complex (no Zn2+)

Lipid II isoglutaminyl synthase (glutamine-hydrolyzing) subunit MurTLipid II isoglutaminyl synthase (glutamine-hydrolyzing) subunit GatD experimental SAS data

Streptococcus pneumoniae lipid II isoglutaminyl synthase MurT:GatD complex (no Zn2+) Rg histogram

Sample:	Lipid II isoglutaminyl synthase (glutamine-hydrolyzing) subunit MurT monomer, 52 kDa Streptococcus pneumoniae (strain … protein Lipid II isoglutaminyl synthase (glutamine-hydrolyzing) subunit GatD monomer, 29 kDa Streptococcus pneumoniae (strain … protein
Buffer:	50 mM Hepes, 10 mM MgCl2, 500 mM NaCl, pH: 7.5
Experiment:	SAXS data collected at EMBL P12, PETRA III on 2019 Jun 23

Unravelling the reaction mechanism of glutamate amidation in Staphylococcus aureus peptidoglycan PhD thesis, NOVA University Lisbon - (2022)
Francisco Miguel Piçarra Leisico, Mertens HD

R_g^Guinier	3.0	nm
D_max	10.0	nm
Volume^Porod	126	nm³

SASDM22 – Staphylococcus aureus lipid II isoglutaminyl synthase MurT:GatD complex

Staphylococcus aureus lipid II isoglutaminyl synthase MurT:GatD complex Rg histogram

Sample:	Lipid II isoglutaminyl synthase (glutamine-hydrolyzing) subunit MurT monomer, 49 kDa Staphylococcus aureus (strain … protein Lipid II isoglutaminyl synthase (glutamine-hydrolyzing) subunit GatD monomer, 28 kDa Staphylococcus aureus (strain … protein
Buffer:	100 mM Tris-HCl, 500 mM NaCl, 10 mM MgCl2, pH: 8.5
Experiment:	SAXS data collected at BM29, ESRF on 2018 Nov 29

Unravelling the reaction mechanism of glutamate amidation in Staphylococcus aureus peptidoglycan PhD thesis, NOVA University Lisbon - (2022)
Francisco Miguel Piçarra Leisico, Mertens HD

R_g^Guinier	3.1	nm
D_max	10.5	nm
Volume^Porod	121	nm³

SASDLS7 – Mycobacterium phage TipsytheTRex immunity repressor bound to DNA

Immunity repressor21mer dsDNA experimental SAS data

Sample:	Immunity repressor monomer, 21 kDa Mycobacterium phage TipsytheTRex protein 21mer dsDNA monomer, 13 kDa DNA
Buffer:	20 mM Tris pH 7.5, 0.5 M NaCl, 1 mM DTT, pH: 7.5
Experiment:	SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2018 Sep 10

A monomeric mycobacteriophage immunity repressor utilizes two domains to recognize an asymmetric DNA sequence. Nat Commun 13(1):4105 (2022)
McGinnis RJ, Brambley CA, Stamey B, Green WC, Gragg KN, Cafferty ER, Terwilliger TC, Hammel M, Hollis TJ, Miller JM, Gainey MD, Wallen JR

R_g^Guinier	2.3	nm
D_max	7.4	nm
Volume^Porod	41	nm³

SASDMK3 – Mycobacterium phage TipsytheTRex apo protein

Immunity repressor experimental SAS data

Sample:	Immunity repressor monomer, 24 kDa Mycobacterium phage TipsytheTRex protein
Buffer:	20 mM Tris pH 7.5, 0.5 M NaCl, 1 mM DTT, pH: 7.5
Experiment:	SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2018 Sep 10

R_g^Guinier	2.3	nm
D_max	9.0	nm
Volume^Porod	43	nm³

SASDML3 – Mycobacterium phage TipsytheTRex immunity repressor bound to 24mer DNA

Immunity repressor24mer dsDNA experimental SAS data

Sample:	Immunity repressor monomer, 21 kDa Mycobacterium phage TipsytheTRex protein 24mer dsDNA monomer, 15 kDa DNA
Buffer:	20 mM Tris pH 7.5, 0.5 M NaCl, 1 mM DTT, pH: 7.5
Experiment:	SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2018 Sep 10

R_g^Guinier	2.4	nm
D_max	9.0	nm
Volume^Porod	43	nm³

SASDMM3 – Mycobacterium phage TipsytheTRex immunity repressor mixed with 13mer DNA

Immunity repressor13mer dsDNA experimental SAS data

Sample:	Immunity repressor monomer, 21 kDa Mycobacterium phage TipsytheTRex protein 13mer dsDNA monomer, 8 kDa DNA
Buffer:	20 mM Tris pH 7.5, 0.5 M NaCl, 1 mM DTT, pH: 7.5
Experiment:	SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2018 Dec 10

R_g^Guinier	2.0	nm
D_max	8.5	nm
Volume^Porod	18	nm³

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