Small Angle Scattering Biological Data Bank SASBDB


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9 hits found for Xi

SASDNH3 – HIV-1 reverse transcriptase L289K mutation at 1 mg/mL

Gag-Pol polyprotein (HIV-1 reverse transcriptase C38V/C280S, L289K truncated to 1 - 556) experimental SAS data

Gag-Pol polyprotein (HIV-1 reverse transcriptase C38V/C280S, L289K truncated to 1 - 556) Kratky plot

Sample:	Gag-Pol polyprotein (HIV-1 reverse transcriptase C38V/C280S, L289K truncated to 1 - 556) monomer, 65 kDa Human immunodeficiency virus … protein
Buffer:	50 mM Bis-Tris pH 6.8, 100 mM NaCl, 1% glycerol, 0.02% w/v NaN3, pH: 6.8
Experiment:	SAXS data collected at 12-ID-B SAXS/WAXS, Advanced Photon Source (APS), Argonne National Laboratory on 2019 Jun 20

Relative domain orientation of the L289K HIV ‐1 reverse transcriptase monomer Protein Science 31(5) (2022)
Xi Z, Ilina T, Guerrero M, Fan L, Sluis‐Cremer N, Wang Y, Ishima R

R_g^Guinier	3.2	nm
D_max	10.7	nm
Volume^Porod	91	nm³

SASDNJ3 – HIV-1 reverse transcriptase L289K mutation at 2 mg/mL

Sample:	Gag-Pol polyprotein (HIV-1 reverse transcriptase C38V/C280S, L289K truncated to 1 - 556) monomer, 65 kDa Human immunodeficiency virus … protein
Buffer:	50 mM Bis-Tris pH 6.8, 100 mM NaCl, 1% glycerol, 0.02% w/v NaN3, pH: 6.8
Experiment:	SAXS data collected at 12-ID-B SAXS/WAXS, Advanced Photon Source (APS), Argonne National Laboratory on 2019 Jun 20

Relative domain orientation of the L289K HIV ‐1 reverse transcriptase monomer Protein Science 31(5) (2022)
Xi Z, Ilina T, Guerrero M, Fan L, Sluis‐Cremer N, Wang Y, Ishima R

R_g^Guinier	3.2	nm
D_max	10.8	nm
Volume^Porod	91	nm³

SASDNK3 – HIV-1 reverse transcriptase L289K mutation at 4.3 mg/mL

Sample:	Gag-Pol polyprotein (HIV-1 reverse transcriptase C38V/C280S, L289K truncated to 1 - 556) monomer, 65 kDa Human immunodeficiency virus … protein
Buffer:	50 mM Bis-Tris pH 6.8, 100 mM NaCl, 1% glycerol, 0.02% w/v NaN3, pH: 6.8
Experiment:	SAXS data collected at 12-ID-B SAXS/WAXS, Advanced Photon Source (APS), Argonne National Laboratory on 2019 Jun 20

Relative domain orientation of the L289K HIV ‐1 reverse transcriptase monomer Protein Science 31(5) (2022)
Xi Z, Ilina T, Guerrero M, Fan L, Sluis‐Cremer N, Wang Y, Ishima R

R_g^Guinier	3.2	nm
D_max	10.7	nm
Volume^Porod	93	nm³

SASDNL3 – HIV-1 reverse transcriptase L289K mutation (extrapolated to zero concentration)

Sample:	Gag-Pol polyprotein (HIV-1 reverse transcriptase C38V/C280S, L289K truncated to 1 - 556) monomer, 65 kDa Human immunodeficiency virus … protein
Buffer:	50 mM Bis-Tris pH 6.8, 100 mM NaCl, 1% glycerol, 0.02% w/v NaN3, pH: 6.8
Experiment:	SAXS data collected at 12-ID-B SAXS/WAXS, Advanced Photon Source (APS), Argonne National Laboratory on 2021 Jun 20

Relative domain orientation of the L289K HIV ‐1 reverse transcriptase monomer Protein Science 31(5) (2022)
Xi Z, Ilina T, Guerrero M, Fan L, Sluis‐Cremer N, Wang Y, Ishima R

R_g^Guinier	3.2	nm
D_max	11.1	nm
Volume^Porod	90	nm³

SASDK48 – Histidine kinase AdeS - DHp-CA Domain

Sample:	Histidine kinase dimer, 51 kDa Acinetobacter baumannii protein
Buffer:	20 mM Tris, 150 mM NaCl, pH: 7.4
Experiment:	SAXS data collected at BL19U2, Shanghai Synchrotron Radiation Facility (SSRF) on 2018 Apr 21

Proteolysis and multimerization regulate signaling along the two-component regulatory system AdeRS. iScience 24(5):102476 (2021)
Ouyang Z, Zheng F, Zhu L, Felix J, Wu D, Wu K, Gutsche I, Wu Y, Hwang PM, She J, Wen Y

R_g^Guinier	2.8	nm
D_max	9.1	nm
Volume^Porod	85	nm³

SASDK58 – Histidine kinase AdeS - cytoplasmic domain

Sample:	Histidine kinase hexamer, 186 kDa Acinetobacter baumannii protein
Buffer:	20 mM Tris, 150 mM NaCl, pH: 7.4
Experiment:	SAXS data collected at BL19U2, Shanghai Synchrotron Radiation Facility (SSRF) on 2019 Jun 19

R_g^Guinier	4.6	nm
D_max	16.3	nm
Volume^Porod	378	nm³

SASDP69 – Acinetobacter baumannii carbonic anhydrase PaaY trimer

Bacterial transferase hexapeptide repeat protein experimental SAS data

Sample:	Bacterial transferase hexapeptide repeat protein trimer, 66 kDa Acinetobacter baumannii (strain … protein
Buffer:	20 mM Tris, 150 mM NaCl, pH: 7.4
Experiment:	SAXS data collected at BL19U2, Shanghai Synchrotron Radiation Facility (SSRF) on 2021 Jan 29

Mechanistic and structural insights into the bifunctional enzyme PaaY from Acinetobacter baumannii. Structure (2023)
Jiao M, He W, Ouyang Z, Qin Q, Guo Y, Zhang J, Bai Y, Guo X, Yu Q, She J, Hwang PM, Zheng F, Wen Y

R_g^Guinier	2.6	nm
D_max	9.0	nm
Volume^Porod	102	nm³

SASDBT9 – Full-length human βB2-crystallin

Beta-crystallin B2 experimental SAS data

Sample:	Beta-crystallin B2 dimer, 46 kDa Homo sapiens protein
Buffer:	25 mM NaPi, 5 mM DTT, 1 mM EDTA,, pH: 6.5
Experiment:	SAXS data collected at 12-ID-B SAXS/WAXS, Advanced Photon Source (APS), Argonne National Laboratory on 2015 Mar 20

Human βB2-Crystallin Forms a Face-en-Face Dimer in Solution: An Integrated NMR and SAXS Study. Structure 25(3):496-505 (2017)
Xi Z, Whitley MJ, Gronenborn AM

R_g^Guinier	2.2	nm
D_max	8.1	nm
Volume^Porod	67	nm³

SASDBU9 – Terminally truncated human βB2-crystallin

Sample:	Beta-crystallin B2 dimer, 42 kDa Homo sapiens protein
Buffer:	25 mM NaPi, 5 mM DTT, 1 mM EDTA,, pH: 6.5
Experiment:	SAXS data collected at 12-ID-B SAXS/WAXS, Advanced Photon Source (APS), Argonne National Laboratory on 2015 Mar 20

Human βB2-Crystallin Forms a Face-en-Face Dimer in Solution: An Integrated NMR and SAXS Study. Structure 25(3):496-505 (2017)
Xi Z, Whitley MJ, Gronenborn AM

R_g^Guinier	2.1	nm
D_max	6.7	nm
Volume^Porod	62	nm³

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