SASBDB entries for UniProt ID:

SASDDL2 – Sinorhizobium meliloti Proline Utilization A (PutA) lowest concentration, 1.00 mg/ml

UniProt ID: F7X6I3 (None-None) Sinorhizobium meliloti (SmPutA)

Sinorhizobium meliloti (SmPutA) experimental SAS data
MES-FOXS model
Sample: Sinorhizobium meliloti (SmPutA) monomer, 132 kDa Sinorhizobium meliloti protein
Buffer: 50 mM Tris, 1% (v/v) glycerol, 0.5 mM THP, and 50 mM NaCl, pH: 7.8
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2014 Mar 27
Structures of Proline Utilization A (PutA) Reveal the Fold and Functions of the Aldehyde Dehydrogenase Superfamily Domain of Unknown Function. J Biol Chem 291(46):24065-24075 (2016)
Luo M, Gamage TT, Arentson BW, Schlasner KN, Becker DF, Tanner JJ
RgGuinier 3.4 nm
Dmax 11.0 nm
VolumePorod 171 nm3

SASDDM2 – Sinorhizobium meliloti Proline Utilization A (PutA) at 2.00 mg/ml

UniProt ID: F7X6I3 (None-None) Sinorhizobium meliloti (SmPutA)

Sinorhizobium meliloti (SmPutA) experimental SAS data
MES-FOXS model
Sample: Sinorhizobium meliloti (SmPutA) monomer, 132 kDa Sinorhizobium meliloti protein
Buffer: 50 mM Tris, 1% (v/v) glycerol, 0.5 mM THP, and 50 mM NaCl, pH: 7.8
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2014 Mar 27
Structures of Proline Utilization A (PutA) Reveal the Fold and Functions of the Aldehyde Dehydrogenase Superfamily Domain of Unknown Function. J Biol Chem 291(46):24065-24075 (2016)
Luo M, Gamage TT, Arentson BW, Schlasner KN, Becker DF, Tanner JJ
RgGuinier 3.8 nm
Dmax 11.9 nm
VolumePorod 225 nm3

SASDDN2 – Sinorhizobium meliloti Proline Utilization A (PutA) at 3.00 mg/ml

UniProt ID: F7X6I3 (None-None) Sinorhizobium meliloti (SmPutA)

Sinorhizobium meliloti (SmPutA) experimental SAS data
MES-FOXS model
Sample: Sinorhizobium meliloti (SmPutA) monomer, 132 kDa Sinorhizobium meliloti protein
Buffer: 50 mM Tris, 1% (v/v) glycerol, 0.5 mM THP, and 50 mM NaCl, pH: 7.8
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2014 Mar 27
Structures of Proline Utilization A (PutA) Reveal the Fold and Functions of the Aldehyde Dehydrogenase Superfamily Domain of Unknown Function. J Biol Chem 291(46):24065-24075 (2016)
Luo M, Gamage TT, Arentson BW, Schlasner KN, Becker DF, Tanner JJ
RgGuinier 3.8 nm
Dmax 11.8 nm
VolumePorod 248 nm3

SASDDP2 – Sinorhizobium meliloti Proline Utilization A (PutA) at high concentration, 4.00 mg/ml

UniProt ID: F7X6I3 (None-None) Sinorhizobium meliloti (SmPutA)

Sinorhizobium meliloti (SmPutA) experimental SAS data
MES-FOXS model
Sample: Sinorhizobium meliloti (SmPutA) monomer, 132 kDa Sinorhizobium meliloti protein
Buffer: 50 mM Tris, 1% (v/v) glycerol, 0.5 mM THP, and 50 mM NaCl, pH: 7.8
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2014 Mar 27
Structures of Proline Utilization A (PutA) Reveal the Fold and Functions of the Aldehyde Dehydrogenase Superfamily Domain of Unknown Function. J Biol Chem 291(46):24065-24075 (2016)
Luo M, Gamage TT, Arentson BW, Schlasner KN, Becker DF, Tanner JJ
RgGuinier 3.9 nm
Dmax 11.9 nm
VolumePorod 277 nm3

SASDDQ2 – EspG3 chaperone from Mycobacterium marinum

UniProt ID: B2HNX0 (None-None) EspG3 chaperone from Mycobacterium marinum M

EspG3 chaperone from Mycobacterium marinum M experimental SAS data
EspG3 chaperone from Mycobacterium marinum M Kratky plot
Sample: EspG3 chaperone from Mycobacterium marinum M monomer, 32 kDa Mycobacterium marinum M protein
Buffer: 20 mM HEPES pH 7.5, 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2014 Mar 17
Structural variability of EspG chaperones from mycobacterial ESX-1, ESX-3 and ESX-5 type VII secretion systems (2018)
Tuukkanen A, Freire D, Chan S, Arbing M, Reed R, Evans T, Zenkeviciutė G, Kim J, Kahng S, Sawaya M, Chaton C, Wilmanns M, Eisenberg D, Parret A, Korotkov K
RgGuinier 2.3 nm
Dmax 8.0 nm

SASDDR2 – EspG1 chaperone from Mycobacterium marinum

UniProt ID: B2HMS9 (None-None) EspG1 from Mycobacterium marinum

EspG1 from Mycobacterium marinum experimental SAS data
EspG1 from Mycobacterium marinum Kratky plot
Sample: EspG1 from Mycobacterium marinum monomer, 30 kDa Mycobacterium marinum protein
Buffer: 20 mM HEPES pH 7.5, 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2014 Mar 17
Structural variability of EspG chaperones from mycobacterial ESX-1, ESX-3 and ESX-5 type VII secretion systems (2018)
Tuukkanen A, Freire D, Chan S, Arbing M, Reed R, Evans T, Zenkeviciutė G, Kim J, Kahng S, Sawaya M, Chaton C, Wilmanns M, Eisenberg D, Parret A, Korotkov K
RgGuinier 2.7 nm
Dmax 9.7 nm

SASDDS2 – EspG3 chaperone from Mycobacter smegmatis

UniProt ID: A0QQ45 (None-None) EspG3 chaperone from Mycobacterium smegmatis

EspG3 chaperone from Mycobacterium smegmatis experimental SAS data
EspG3 chaperone from Mycobacterium smegmatis Kratky plot
Sample: EspG3 chaperone from Mycobacterium smegmatis monomer, 32 kDa Mycobacterium smegmatis protein
Buffer: 20 mM HEPES pH 7.5, 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2014 Mar 17
Structural variability of EspG chaperones from mycobacterial ESX-1, ESX-3 and ESX-5 type VII secretion systems (2018)
Tuukkanen A, Freire D, Chan S, Arbing M, Reed R, Evans T, Zenkeviciutė G, Kim J, Kahng S, Sawaya M, Chaton C, Wilmanns M, Eisenberg D, Parret A, Korotkov K
RgGuinier 2.5 nm
Dmax 8.6 nm

SASDDT2 – EspG3 chaperone from Mycobacterium tuberculosis

UniProt ID: P9WJC6 (None-None) EspG3 chaperone from Mycobacterium tuberculosis

EspG3 chaperone from Mycobacterium tuberculosis experimental SAS data
EspG3 chaperone from Mycobacterium tuberculosis Kratky plot
Sample: EspG3 chaperone from Mycobacterium tuberculosis, 34 kDa Mycobacterium tuberculosis protein
Buffer: 20 mM HEPES pH 7.5, 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2014 Mar 17
Structural variability of EspG chaperones from mycobacterial ESX-1, ESX-3 and ESX-5 type VII secretion systems (2018)
Tuukkanen A, Freire D, Chan S, Arbing M, Reed R, Evans T, Zenkeviciutė G, Kim J, Kahng S, Sawaya M, Chaton C, Wilmanns M, Eisenberg D, Parret A, Korotkov K
RgGuinier 2.5 nm
Dmax 9.0 nm

SASDDU2 – EspG3 chaperone from Mycobacterium smegmatis (Sel-Met labelled)

UniProt ID: A0QQ45 (None-None) EspG3 chaperone from Mycobacterium smegmatis

EspG3 chaperone from Mycobacterium smegmatis experimental SAS data
EspG3 chaperone from Mycobacterium smegmatis Kratky plot
Sample: EspG3 chaperone from Mycobacterium smegmatis monomer, 32 kDa Mycobacterium smegmatis protein
Buffer: 20 mM HEPES pH 7.5, 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2014 Mar 17
Structural variability of EspG chaperones from mycobacterial ESX-1, ESX-3 and ESX-5 type VII secretion systems (2018)
Tuukkanen A, Freire D, Chan S, Arbing M, Reed R, Evans T, Zenkeviciutė G, Kim J, Kahng S, Sawaya M, Chaton C, Wilmanns M, Eisenberg D, Parret A, Korotkov K
RgGuinier 2.6 nm
Dmax 9.2 nm

SASDDV2 – EspG5 chaperone from Mycobacterium tuberculosis

UniProt ID: O53943 (None-None) EspG5 chaperone from Mycobacterium tuberculosis

EspG5 chaperone from Mycobacterium tuberculosis experimental SAS data
EspG5 chaperone from Mycobacterium tuberculosis Rg histogram
Sample: EspG5 chaperone from Mycobacterium tuberculosis monomer, 32 kDa Mycobacterium tuberculosis protein
Buffer: 20 mM HEPES pH 7.5, 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2015 Jan 12
Structural variability of EspG chaperones from mycobacterial ESX-1, ESX-3 and ESX-5 type VII secretion systems (2018)
Tuukkanen A, Freire D, Chan S, Arbing M, Reed R, Evans T, Zenkeviciutė G, Kim J, Kahng S, Sawaya M, Chaton C, Wilmanns M, Eisenberg D, Parret A, Korotkov K
RgGuinier 2.4 nm
Dmax 8.0 nm