Browse by MODEL: No model

SASDUY4 – Calcium/calmodulin-dependent protein kinase type II alpha (CaMKIIα) WT hub domain with HOCPCA

Calcium/calmodulin-dependent protein kinase type II subunit alpha3-hydroxycyclopent-1-enecarboxylic acid experimental SAS data
Calcium/calmodulin-dependent protein kinase type II subunit alpha 3-hydroxycyclopent-1-enecarboxylic acid Kratky plot
Sample: Calcium/calmodulin-dependent protein kinase type II subunit alpha dodecamer, 186 kDa Homo sapiens protein
3-hydroxycyclopent-1-enecarboxylic acid monomer, 0 kDa
Buffer: 20 mM MES, 150 mM NaCl, 1 mM DTT, 1 mM HOCPCA, pH: 6
Experiment: SAXS data collected at Xenocs BioXolver L with MetalJet, University of Copenhagen, Department of Drug Design and Pharmacology on 2020 Nov 19
Ligand‐induced CaMKIIα hub Trp403 flip, hub domain stacking, and modulation of kinase activity Protein Science 33(10) (2024)
Narayanan D, Larsen A, Gauger S, Adafia R, Hammershøi R, Hamborg L, Bruus‐Jensen J, Griem‐Krey N, Gee C, Frølund B, Stratton M, Kuriyan J, Kastrup J, Langkilde A, Wellendorph P, Solbak S
RgGuinier 4.1 nm
Dmax 12.7 nm
VolumePorod 310 nm3

SASDUZ4 – Calcium/calmodulin-dependent protein kinase type II alpha (CaMKIIα) W403L hub domain

Calcium/calmodulin-dependent protein kinase type II subunit alpha (W403L) experimental SAS data
Calcium/calmodulin-dependent protein kinase type II subunit alpha (W403L) Kratky plot
Sample: Calcium/calmodulin-dependent protein kinase type II subunit alpha (W403L) dodecamer, 185 kDa Homo sapiens protein
Buffer: 20 mM MES, 150 mM NaCl, 1 mM DTT, pH: 6
Experiment: SAXS data collected at EMBL P12, PETRA III on 2023 Mar 17
Ligand‐induced CaMKIIα hub Trp403 flip, hub domain stacking, and modulation of kinase activity Protein Science 33(10) (2024)
Narayanan D, Larsen A, Gauger S, Adafia R, Hammershøi R, Hamborg L, Bruus‐Jensen J, Griem‐Krey N, Gee C, Frølund B, Stratton M, Kuriyan J, Kastrup J, Langkilde A, Wellendorph P, Solbak S
RgGuinier 4.7 nm
Dmax 16.5 nm
VolumePorod 358 nm3

SASDU25 – Calcium/calmodulin-dependent protein kinase type II alpha (CaMKIIα) W403L hub domain with PIPA

Calcium/calmodulin-dependent protein kinase type II subunit alpha (W403L)2-(6-(4-chlorophenyl)imidazo[1,2-b]pyridazine-2-yl)acetic acid experimental SAS data
Calcium/calmodulin-dependent protein kinase type II subunit alpha (W403L) 2-(6-(4-chlorophenyl)imidazo[1,2-b]pyridazine-2-yl)acetic acid Kratky plot
Sample: Calcium/calmodulin-dependent protein kinase type II subunit alpha (W403L) dodecamer, 185 kDa Homo sapiens protein
2-(6-(4-chlorophenyl)imidazo[1,2-b]pyridazine-2-yl)acetic acid monomer, 0 kDa
Buffer: 20 mM MES, 150 mM NaCl, 1 mM DTT, 200 µM PIPA, pH: 6
Experiment: SAXS data collected at EMBL P12, PETRA III on 2023 Mar 17
Ligand‐induced CaMKIIα hub Trp403 flip, hub domain stacking, and modulation of kinase activity Protein Science 33(10) (2024)
Narayanan D, Larsen A, Gauger S, Adafia R, Hammershøi R, Hamborg L, Bruus‐Jensen J, Griem‐Krey N, Gee C, Frølund B, Stratton M, Kuriyan J, Kastrup J, Langkilde A, Wellendorph P, Solbak S
RgGuinier 4.4 nm
Dmax 15.0 nm
VolumePorod 334 nm3

SASDU35 – Calcium/calmodulin-dependent protein kinase type II alpha (CaMKIIα) W403L hub domain with 5-HDC

Calcium/calmodulin-dependent protein kinase type II subunit alpha (W403L)5-hydroxydiclofenac experimental SAS data
Calcium/calmodulin-dependent protein kinase type II subunit alpha (W403L) 5-hydroxydiclofenac Kratky plot
Sample: Calcium/calmodulin-dependent protein kinase type II subunit alpha (W403L) dodecamer, 185 kDa Homo sapiens protein
5-hydroxydiclofenac monomer, 0 kDa
Buffer: 20 mM MES, 150 mM NaCl, 1 mM DTT, 100 µM 5-HDC, pH: 6
Experiment: SAXS data collected at Xenocs BioXolver L, Département de Biochimie, Université de Montréal on 2022 Dec 15
Ligand‐induced CaMKIIα hub Trp403 flip, hub domain stacking, and modulation of kinase activity Protein Science 33(10) (2024)
Narayanan D, Larsen A, Gauger S, Adafia R, Hammershøi R, Hamborg L, Bruus‐Jensen J, Griem‐Krey N, Gee C, Frølund B, Stratton M, Kuriyan J, Kastrup J, Langkilde A, Wellendorph P, Solbak S
RgGuinier 4.4 nm
Dmax 15.0 nm
VolumePorod 335 nm3

SASDU55 – Calcium/calmodulin-dependent protein kinase type II alpha (CaMKIIα) 6x hub domain

Calcium/calmodulin-dependent protein kinase type II subunit alpha (T354N, E355Q, T412N, I414M, I464H, F467M) experimental SAS data
Calcium/calmodulin-dependent protein kinase type II subunit alpha (T354N, E355Q, T412N, I414M, I464H, F467M) Kratky plot
Sample: Calcium/calmodulin-dependent protein kinase type II subunit alpha (T354N, E355Q, T412N, I414M, I464H, F467M) 14-mer, 217 kDa Homo sapiens protein
Buffer: 20 mM MES, 150 mM NaCl, 1 mM DTT, pH: 6
Experiment: SAXS data collected at Xenocs BioXolver L with MetalJet, University of Copenhagen, Department of Drug Design and Pharmacology on 2020 Nov 19
Ligand‐induced CaMKIIα hub Trp403 flip, hub domain stacking, and modulation of kinase activity Protein Science 33(10) (2024)
Narayanan D, Larsen A, Gauger S, Adafia R, Hammershøi R, Hamborg L, Bruus‐Jensen J, Griem‐Krey N, Gee C, Frølund B, Stratton M, Kuriyan J, Kastrup J, Langkilde A, Wellendorph P, Solbak S
RgGuinier 4.5 nm
Dmax 14.5 nm
VolumePorod 313 nm3

SASDU65 – Calcium/calmodulin-dependent protein kinase type II alpha (CaMKIIα) 6x hub domain with PIPA

Calcium/calmodulin-dependent protein kinase type II subunit alpha (T354N, E355Q, T412N, I414M, I464H, F467M)2-(6-(4-chlorophenyl)imidazo[1,2-b]pyridazine-2-yl)acetic acid experimental SAS data
Calcium/calmodulin-dependent protein kinase type II subunit alpha (T354N, E355Q, T412N, I414M, I464H, F467M) 2-(6-(4-chlorophenyl)imidazo[1,2-b]pyridazine-2-yl)acetic acid Kratky plot
Sample: Calcium/calmodulin-dependent protein kinase type II subunit alpha (T354N, E355Q, T412N, I414M, I464H, F467M) 14-mer, 217 kDa Homo sapiens protein
2-(6-(4-chlorophenyl)imidazo[1,2-b]pyridazine-2-yl)acetic acid monomer, 0 kDa
Buffer: 20 mM MES, 150 mM NaCl, 1 mM DTT, 200 µM PIPA, pH: 6
Experiment: SAXS data collected at Xenocs BioXolver L with MetalJet, University of Copenhagen, Department of Drug Design and Pharmacology on 2022 Nov 30
Ligand‐induced CaMKIIα hub Trp403 flip, hub domain stacking, and modulation of kinase activity Protein Science 33(10) (2024)
Narayanan D, Larsen A, Gauger S, Adafia R, Hammershøi R, Hamborg L, Bruus‐Jensen J, Griem‐Krey N, Gee C, Frølund B, Stratton M, Kuriyan J, Kastrup J, Langkilde A, Wellendorph P, Solbak S
RgGuinier 4.7 nm
Dmax 20.0 nm
VolumePorod 375 nm3

SASDU75 – Calcium/calmodulin-dependent protein kinase type II alpha (CaMKIIα) 6x hub domain with 5-HDC

Calcium/calmodulin-dependent protein kinase type II subunit alpha (T354N, E355Q, T412N, I414M, I464H, F467M)5-hydroxydiclofenac experimental SAS data
Calcium/calmodulin-dependent protein kinase type II subunit alpha (T354N, E355Q, T412N, I414M, I464H, F467M) 5-hydroxydiclofenac Kratky plot
Sample: Calcium/calmodulin-dependent protein kinase type II subunit alpha (T354N, E355Q, T412N, I414M, I464H, F467M) 14-mer, 217 kDa Homo sapiens protein
5-hydroxydiclofenac monomer, 0 kDa
Buffer: 20 mM MES, 150 mM NaCl, 1 mM DTT, 100 µM 5-HDC, pH: 6
Experiment: SAXS data collected at Xenocs BioXolver L with MetalJet, University of Copenhagen, Department of Drug Design and Pharmacology on 2020 Nov 19
Ligand‐induced CaMKIIα hub Trp403 flip, hub domain stacking, and modulation of kinase activity Protein Science 33(10) (2024)
Narayanan D, Larsen A, Gauger S, Adafia R, Hammershøi R, Hamborg L, Bruus‐Jensen J, Griem‐Krey N, Gee C, Frølund B, Stratton M, Kuriyan J, Kastrup J, Langkilde A, Wellendorph P, Solbak S
RgGuinier 4.7 nm
Dmax 18.5 nm
VolumePorod 366 nm3

SASDV72 – Human Haemoglobin (Sigma-Aldrich) in 100mM Sodium Phosphate buffer, pH=7.0, c=5mg/ml, 1 day after SEC

Hemoglobin subunit alphaHemoglobin subunit betaProtoporphyrin IX containing fe experimental SAS data
Hemoglobin subunit alpha Hemoglobin subunit beta Protoporphyrin IX containing fe Kratky plot
Sample: Hemoglobin subunit alpha monomer, 15 kDa Homo sapiens protein
Hemoglobin subunit beta monomer, 16 kDa Homo sapiens protein
Protoporphyrin IX containing fe monomer, 1 kDa
Buffer: 100 mM Sodium Phosphate, pH: 7
Experiment: SAXS data collected at Anton Paar SAXSpoint 2.0, Institute of Biotechnology, Czech Academy of Sciences/Centre of Molecular Structure on 2022 Sep 30
Hemoglobin–PEG Interactions Probed by Small-Angle X-ray Scattering: Insights for Crystallization and Diagnostics Applications The Journal of Physical Chemistry B (2024)
Baranova I, Angelova A, Stransky J, Andreasson J, Angelov B
RgGuinier 2.4 nm
Dmax 6.7 nm
VolumePorod 103 nm3

SASDV82 – Human Haemoglobin (Sigma-Aldrich) with 5% (w/v) PEG600 in 100mM Sodium Phosphate buffer pH=7.0, c=5 mg/ml

Hemoglobin subunit alphaHemoglobin subunit betaProtoporphyrin IX containing fe experimental SAS data
Hemoglobin subunit alpha Hemoglobin subunit beta Protoporphyrin IX containing fe Kratky plot
Sample: Hemoglobin subunit alpha monomer, 15 kDa Homo sapiens protein
Hemoglobin subunit beta monomer, 16 kDa Homo sapiens protein
Protoporphyrin IX containing fe monomer, 1 kDa
Buffer: 100mM Sodium Phosphate buffer with 5% (w/v) PEG600, pH: 7
Experiment: SAXS data collected at Anton Paar SAXSpoint 2.0, Institute of Biotechnology, Czech Academy of Sciences/Centre of Molecular Structure on 2022 Sep 30
Hemoglobin–PEG Interactions Probed by Small-Angle X-ray Scattering: Insights for Crystallization and Diagnostics Applications The Journal of Physical Chemistry B (2024)
Baranova I, Angelova A, Stransky J, Andreasson J, Angelov B
RgGuinier 2.4 nm
Dmax 6.7 nm
VolumePorod 105 nm3

SASDV92 – Human Haemoglobin (Sigma-Aldrich) with 10% (w/v) PEG600 in 100mM Sodium Phosphate buffer pH=7.0, c=5 mg/ml

Hemoglobin subunit alphaHemoglobin subunit betaProtoporphyrin IX containing fe experimental SAS data
Hemoglobin subunit alpha Hemoglobin subunit beta Protoporphyrin IX containing fe Kratky plot
Sample: Hemoglobin subunit alpha monomer, 15 kDa Homo sapiens protein
Hemoglobin subunit beta monomer, 16 kDa Homo sapiens protein
Protoporphyrin IX containing fe monomer, 1 kDa
Buffer: 100mM Sodium Phosphate buffer with 10% (w/v) PEG600, pH: 7
Experiment: SAXS data collected at Anton Paar SAXSpoint 2.0, Institute of Biotechnology, Czech Academy of Sciences/Centre of Molecular Structure on 2022 Sep 30
Hemoglobin–PEG Interactions Probed by Small-Angle X-ray Scattering: Insights for Crystallization and Diagnostics Applications The Journal of Physical Chemistry B (2024)
Baranova I, Angelova A, Stransky J, Andreasson J, Angelov B
RgGuinier 2.4 nm
Dmax 7.2 nm
VolumePorod 113 nm3