Small Angle Scattering Biological Data Bank SASBDB

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SASDVU6 – SARS-CoV-2 N-protein (N1-245; amino acids 1-245): 167 µM

Sample:	Nucleoprotein dimer, 55 kDa Severe acute respiratory … protein
Buffer:	100 mM Tris-HCl, 150 mM NaCl, 1 mM EDTA, pH: 8
Experiment:	SAXS data collected at B21, Diamond Light Source on 2022 May 13

Dynamic ensembles of SARS-CoV-2 N-protein reveal head-to-head coiled-coil-driven oligomerization and phase separation. Nucleic Acids Res 53(11) (2025)
Hernandez G, Martins ML, Fernandes NP, Veloso T, Lopes J, Gomes T, Cordeiro TN

R_g^Guinier	5.2	nm
D_max	20.5	nm
Volume^Porod	121	nm³

SASDV98 – Full-length N(5)-hydroxyornithine:cis-anhydromevalonyl coenzyme A-N(5)-transacylase sidF

N(5)-hydroxyornithine:cis-anhydromevalonyl coenzyme A-N(5)-transacylase sidF experimental SAS data

Full-length N(5)-hydroxyornithine:cis-anhydromevalonyl coenzyme A-N(5)-transacylase sidF Rg histogram

Sample:	N(5)-hydroxyornithine:cis-anhydromevalonyl coenzyme A-N(5)-transacylase sidF tetramer, 223 kDa Aspergillus fumigatus (strain … protein
Buffer:	50 mM Tris, 200 mM NaCl, pH: 8
Experiment:	SAXS data collected at Anton Paar SAXSpoint 2.0, Institute of Biotechnology, Czech Academy of Sciences/Centre of Molecular Structure on 2022 Jul 7

SidF, a dual substrate N5-acetyl-N5-hydroxy-L-ornithine transacetylase involved in Aspergillus fumigatus siderophore biosynthesis Journal of Structural Biology: X 11:100119 (2025)
Poonsiri T, Stransky J, Demitri N, Haas H, Cianci M, Benini S

R_g^Guinier	4.0	nm
D_max	19.0	nm
Volume^Porod	412	nm³

SASDVA8 – The N-terminal domain of N(5)-hydroxyornithine:cis-anhydromevalonyl coenzyme A-N(5)-transacylase sidF

The N-terminal domain of N(5)-hydroxyornithine:cis-anhydromevalonyl coenzyme A-N(5)-transacylase sidF Rg histogram

Sample:	N(5)-hydroxyornithine:cis-anhydromevalonyl coenzyme A-N(5)-transacylase sidF monomer, 25 kDa Aspergillus fumigatus (strain … protein
Buffer:	50 mM Tris, 200 mM NaCl, pH: 8
Experiment:	SAXS data collected at Anton Paar SAXSpoint 2.0, Institute of Biotechnology, Czech Academy of Sciences/Centre of Molecular Structure on 2023 Jan 18

R_g^Guinier	2.2	nm
D_max	8.9	nm
Volume^Porod	30	nm³

SASDVB8 – C-terminal truncation mutant of N(5)-hydroxyornithine:cis-anhydromevalonyl coenzyme A-N(5)-transacylase sidF

N(5)-hydroxyornithine:cis-anhydromevalonyl coenzyme A-N(5)-transacylase sidF (Δ444-462) experimental SAS data

Sample:	N(5)-hydroxyornithine:cis-anhydromevalonyl coenzyme A-N(5)-transacylase sidF (Δ444-462) dimer, 107 kDa Aspergillus fumigatus (strain … protein
Buffer:	50 mM Tris, 200 mM NaCl, pH: 8
Experiment:	SAXS data collected at Anton Paar SAXSpoint 2.0, Institute of Biotechnology, Czech Academy of Sciences/Centre of Molecular Structure on 2023 Jan 18

R_g^Guinier	3.5	nm
D_max	15.0	nm
Volume^Porod	189	nm³

SASDVF8 – S9 peptidase form Mycobacterium phlei (8 mg/ml)

Sample:	Peptidase S9 tetramer, 304 kDa Mycolicibacterium phlei DSM … protein
Buffer:	10 mM Tris-HCl, 135 mM NaCl, pH: 8
Experiment:	SAXS data collected at BL-18, INDUS-2 on 2024 Mar 21

Structural and Functional Investigation of Putative Peptidase from Mycolicibacterium phlei : An Exclusive Endopeptidase among S9C Subfamily Biochemistry (2025)
Chandravanshi K, Jamdar S, Singh R, Kumar A, Mahato A, Agrawal R, Kumar S, Kumar A, Makde R

R_g^Guinier	5.2	nm
D_max	15.8	nm
Volume^Porod	559	nm³

SASDVG8 – S9 peptidase form Mycobacterium phlei (6 mg/ml)

Sample:	Peptidase S9 tetramer, 304 kDa Mycolicibacterium phlei DSM … protein
Buffer:	10 mM Tris-HCl, 135 mM NaCl, pH: 8
Experiment:	SAXS data collected at BL-18, INDUS-2 on 2024 Mar 21

R_g^Guinier	5.0	nm
D_max	15.7	nm
Volume^Porod	546	nm³

SASDVH8 – S9 peptidase form Mycobacterium phlei (4 mg/ml)

Sample:	Peptidase S9 tetramer, 304 kDa Mycolicibacterium phlei DSM … protein
Buffer:	10 mM Tris-HCl, 135 mM NaCl, pH: 8
Experiment:	SAXS data collected at BL-18, INDUS-2 on 2024 Mar 21

R_g^Guinier	5.1	nm
D_max	16.2	nm
Volume^Porod	563	nm³

SASDSV2 – spikemoss tandem zinc finger (TZF) domain, pH 8 at 5.5 mg/mL

C3H1-type domain-containing protein experimental SAS data

C3H1-type domain-containing protein Kratky plot

Sample:	C3H1-type domain-containing protein monomer, 8 kDa Selaginella moellendorffii protein
Buffer:	20 mM sodium phosphate, 100 mM KCl, 25 µM ZnSO4, 2 mM β-mercaptoethanol, 5 % glycerol, pH: 8
Experiment:	SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2016 Nov 9

Solution scattering of the tandem zinc finger (TZF) domain from the tristetraprolin (TTP) family member found in Selaginella moellendorffii (spikemoss) in the presence and absence of 9-mer RNA
Stephanie Hicks

R_g^Guinier	1.8	nm
D_max	7.3	nm
Volume^Porod	15	nm³

SASDSW2 – spikemoss tandem zinc finger (TZF) domain, pH 8 at 4.1 mg/mL

Sample:	C3H1-type domain-containing protein monomer, 8 kDa Selaginella moellendorffii protein
Buffer:	20 mM sodium phosphate, 100 mM KCl, 25 µM ZnSO4, 2 mM β-mercaptoethanol, 5 % glycerol, pH: 8
Experiment:	SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2016 Nov 9

R_g^Guinier	1.7	nm
D_max	7.1	nm
Volume^Porod	14	nm³

SASDSX2 – spikemoss tandem zinc finger (TZF) domain, pH 8 at 2.75 mg/mL

Sample:	C3H1-type domain-containing protein monomer, 8 kDa Selaginella moellendorffii protein
Buffer:	20 mM sodium phosphate, 100 mM KCl, 25 µM ZnSO4, 2 mM β-mercaptoethanol, 5 % glycerol, pH: 8
Experiment:	SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2016 Nov 9

R_g^Guinier	1.7	nm
D_max	7.1	nm
Volume^Porod	14	nm³

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