SASBDB entries for UniProt ID:

SASDTM7 – RECQ like helicase 5 fragment (amino acids 625-825; 0.2 mg/ml)

UniProt ID: O94762 (625-825) ATP-dependent DNA helicase Q5

ATP-dependent DNA helicase Q5 experimental SAS data
ATP-dependent DNA helicase Q5 Kratky plot
Sample: ATP-dependent DNA helicase Q5, 21 kDa Homo sapiens protein
Buffer: 25 mM HEPES, 200 mM NaCl, 1 mM DTT, pH: 7.5
Experiment: SAXS data collected at Rigaku BioSAXS-2000, CEITEC on 2023 Apr 19
Mechanisms of transcription attenuation and condensation of RNA polymerase II by RECQ5
Tomas Klumpler
RgGuinier 3.7 nm
Dmax 9.3 nm
VolumePorod 73 nm3

SASDTN7 – RECQ like helicase 5 fragment (amino acids 625-825; 0.4 mg/ml)

UniProt ID: O94762 (1-991) ATP-dependent DNA helicase Q5

ATP-dependent DNA helicase Q5 experimental SAS data
ATP-dependent DNA helicase Q5 Kratky plot
Sample: ATP-dependent DNA helicase Q5, 109 kDa Homo sapiens protein
Buffer: 25 mM HEPES, 200 mM NaCl, 1 mM DTT, pH: 7.5
Experiment: SAXS data collected at Rigaku BioSAXS-2000, CEITEC on 2023 Apr 19
Mechanisms of transcription attenuation and condensation of RNA polymerase II by RECQ5
Tomas Klumpler
RgGuinier 3.9 nm
Dmax 10.1 nm
VolumePorod 91 nm3

SASDTP7 – RECQ like helicase 5 fragment (amino acids 625-825; 0.6 mg/ml)

UniProt ID: O94762 (1-991) ATP-dependent DNA helicase Q5

ATP-dependent DNA helicase Q5 experimental SAS data
ATP-dependent DNA helicase Q5 Kratky plot
Sample: ATP-dependent DNA helicase Q5, 109 kDa Homo sapiens protein
Buffer: 25 mM HEPES, 200 mM NaCl, 1 mM DTT, pH: 7.5
Experiment: SAXS data collected at Rigaku BioSAXS-2000, CEITEC on 2023 Apr 19
Mechanisms of transcription attenuation and condensation of RNA polymerase II by RECQ5
Tomas Klumpler
RgGuinier 4.3 nm
Dmax 11.2 nm
VolumePorod 116 nm3

SASDTQ7 – RECQ like helicase 5 fragment (amino acids 625-825; 0.8 mg/ml)

UniProt ID: O94762 (1-991) ATP-dependent DNA helicase Q5

ATP-dependent DNA helicase Q5 experimental SAS data
ATP-dependent DNA helicase Q5 Kratky plot
Sample: ATP-dependent DNA helicase Q5, 109 kDa Homo sapiens protein
Buffer: 25 mM HEPES, 200 mM NaCl, 1 mM DTT, pH: 7.5
Experiment: SAXS data collected at Rigaku BioSAXS-2000, CEITEC on 2023 Apr 19
Mechanisms of transcription attenuation and condensation of RNA polymerase II by RECQ5
Tomas Klumpler
RgGuinier 4.6 nm
Dmax 13.2 nm
VolumePorod 102 nm3

SASDTR7 – RECQ like helicase 5 fragment (amino acids 625-825; 1.0 mg/ml)

UniProt ID: O94762 (1-991) ATP-dependent DNA helicase Q5

ATP-dependent DNA helicase Q5 experimental SAS data
ATP-dependent DNA helicase Q5 Kratky plot
Sample: ATP-dependent DNA helicase Q5, 109 kDa Homo sapiens protein
Buffer: 25 mM HEPES, 200 mM NaCl, 1 mM DTT, pH: 7.5
Experiment: SAXS data collected at Rigaku BioSAXS-2000, CEITEC on 2023 Apr 19
Mechanisms of transcription attenuation and condensation of RNA polymerase II by RECQ5
Tomas Klumpler
RgGuinier 5.7 nm
Dmax 16.2 nm
VolumePorod 150 nm3

SASDTS7 – Bovine Lactoferrin

UniProt ID: Q6LBN7 (1-681) Lactoferrin

Lactoferrin experimental SAS data
Lactoferrin Kratky plot
Sample: Lactoferrin monomer, 75 kDa Bos taurus protein
Buffer: 20 mM HEPES, 150 mM NaCl, pH: 7.4
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2021 Jun 23
A secreted bacterial protein protects bacteria from cationic antimicrobial peptides by entrapment in phase separated droplets PNAS Nexus (2024)
Ostan N, Cole G, Wang F, Reichheld S, Moore G, Pan C, Yu R, Lai C, Sharpe S, Lee H, Schryvers A, Moraes T
RgGuinier 3.2 nm
Dmax 11.5 nm
VolumePorod 117 nm3

SASDTT7 – Lactoferrin binding protein B

UniProt ID: K7P8F3 (41-900) Transferrin-binding protein B

Transferrin-binding protein B experimental SAS data
Transferrin-binding protein B Kratky plot
Sample: Transferrin-binding protein B monomer, 97 kDa Moraxella bovis protein
Buffer: 20 mM HEPES, 150 mM NaCl, pH: 7.4
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2021 Jun 23
A secreted bacterial protein protects bacteria from cationic antimicrobial peptides by entrapment in phase separated droplets PNAS Nexus (2024)
Ostan N, Cole G, Wang F, Reichheld S, Moore G, Pan C, Yu R, Lai C, Sharpe S, Lee H, Schryvers A, Moraes T
RgGuinier 3.7 nm
Dmax 12.4 nm
VolumePorod 130 nm3

SASDTU7 – Lactoferrin binding protein B (C-terminal alpha helical domain)

UniProt ID: K7P8F3 (464-725) Transferrin-binding protein B

Transferrin-binding protein B experimental SAS data
Transferrin-binding protein B Kratky plot
Sample: Transferrin-binding protein B monomer, 32 kDa Moraxella bovis protein
Buffer: 20 mM HEPES, 150 mM NaCl, pH: 7.4
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2021 Jun 23
A secreted bacterial protein protects bacteria from cationic antimicrobial peptides by entrapment in phase separated droplets PNAS Nexus (2024)
Ostan N, Cole G, Wang F, Reichheld S, Moore G, Pan C, Yu R, Lai C, Sharpe S, Lee H, Schryvers A, Moraes T
RgGuinier 3.2 nm
Dmax 11.9 nm
VolumePorod 49 nm3

SASDTV7 – Lactoferrin binding protein B (C-terminal alpha helical domain) bound to bovine lactoferrin

UniProt ID: Q6LBN7 (1-681) Lactoferrin

UniProt ID: K7P8F3 (464-725) Transferrin-binding protein B

LactoferrinTransferrin-binding protein B experimental SAS data
Lactoferrin Transferrin-binding protein B Kratky plot
Sample: Lactoferrin monomer, 75 kDa Bos taurus protein
Transferrin-binding protein B monomer, 32 kDa Moraxella bovis protein
Buffer: 20 mM HEPES, 150 mM NaCl, pH: 7.4
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2021 Jun 23
A secreted bacterial protein protects bacteria from cationic antimicrobial peptides by entrapment in phase separated droplets PNAS Nexus (2024)
Ostan N, Cole G, Wang F, Reichheld S, Moore G, Pan C, Yu R, Lai C, Sharpe S, Lee H, Schryvers A, Moraes T
RgGuinier 5.6 nm
Dmax 20.3 nm
VolumePorod 318 nm3

SASDTW7 – Heterogeneous nuclear ribonucleoprotein A1-A (hnRNP A1-A; SEC-SAXS, July 2022)

UniProt ID: P09651-2 (2-320) Isoform A1-A of Heterogeneous nuclear ribonucleoprotein A1 (C43S/C175S)

Isoform A1-A of Heterogeneous nuclear ribonucleoprotein A1 (C43S/C175S) experimental SAS data
Isoform A1-A of Heterogeneous nuclear ribonucleoprotein A1 (C43S/C175S) Kratky plot
Sample: Isoform A1-A of Heterogeneous nuclear ribonucleoprotein A1 (C43S/C175S) monomer, 34 kDa Homo sapiens protein
Buffer: 100 mM HEPES, 350 mM NaCl, 0.5 mM EDTA, pH: 7.5
Experiment: SAXS data collected at 12-ID-B, Advanced Photon Source (APS), Argonne National Laboratory on 2022 Jul 7
Thermodynamic coupling of the tandem RRM domains of hnRNP A1 underlie its pleiotropic RNA binding functions. Sci Adv 10(28):eadk6580 (2024)
Levengood JD, Potoyan D, Penumutchu S, Kumar A, Zhou Q, Wang Y, Hansen AL, Kutluay S, Roche J, Tolbert BS
RgGuinier 2.9 nm
Dmax 12.0 nm
VolumePorod 54 nm3