author_facet Braun, Thomas
Philippsen, Ansgar
Wirtz, Sabine
Borgnia, Mario J.
Agre, Peter
Kühlbrandt, Werner
Engel, Andreas
Stahlberg, Henning
Braun, Thomas
Philippsen, Ansgar
Wirtz, Sabine
Borgnia, Mario J.
Agre, Peter
Kühlbrandt, Werner
Engel, Andreas
Stahlberg, Henning
author Braun, Thomas
Philippsen, Ansgar
Wirtz, Sabine
Borgnia, Mario J.
Agre, Peter
Kühlbrandt, Werner
Engel, Andreas
Stahlberg, Henning
spellingShingle Braun, Thomas
Philippsen, Ansgar
Wirtz, Sabine
Borgnia, Mario J.
Agre, Peter
Kühlbrandt, Werner
Engel, Andreas
Stahlberg, Henning
EMBO reports
The 3.7 Å projection map of the glycerol facilitator GlpF: a variant of the aquaporin tetramer
Genetics
Molecular Biology
Biochemistry
author_sort braun, thomas
spelling Braun, Thomas Philippsen, Ansgar Wirtz, Sabine Borgnia, Mario J. Agre, Peter Kühlbrandt, Werner Engel, Andreas Stahlberg, Henning 1469-221X 1469-3178 Springer Science and Business Media LLC Genetics Molecular Biology Biochemistry http://dx.doi.org/10.1093/embo-reports/kvd022 <jats:p>GlpF, the glycerol facilitator protein of <jats:italic>Escherichia coli</jats:italic>, is an archetypal member of the aquaporin superfamily. To assess its structure, recombinant histidine‐tagged protein was overexpressed, solubilized in octylglucoside and purified to homogeneity. Negative stain electron microscopy of solubilized GlpF protein revealed a tetrameric structure of ∼80 Å side length. Scanning transmission electron microscopy yielded a mass of 170 kDa, corroborating the tetrameric nature of GlpF. Reconstitution of GlpF in the presence of lipids produced highly ordered two‐dimensional crystals, which diffracted electrons to 3.6 Å resolution. Cryoelectron microscopy provided a 3.7 Å projection map exhibiting a unit cell comprised of two tetramers. In projection, GlpF is similar to AQP1, the erythrocyte water channel. However, the major density minimum within each monomer is distinctly larger in GlpF than in AQP1.</jats:p> The 3.7 Å projection map of the glycerol facilitator GlpF: a variant of the aquaporin tetramer EMBO reports
doi_str_mv 10.1093/embo-reports/kvd022
facet_avail Online
Free
finc_class_facet Biologie
Chemie und Pharmazie
format ElectronicArticle
fullrecord blob:ai-49-aHR0cDovL2R4LmRvaS5vcmcvMTAuMTA5My9lbWJvLXJlcG9ydHMva3ZkMDIy
id ai-49-aHR0cDovL2R4LmRvaS5vcmcvMTAuMTA5My9lbWJvLXJlcG9ydHMva3ZkMDIy
institution DE-Zi4
DE-Gla1
DE-15
DE-Pl11
DE-Rs1
DE-14
DE-105
DE-Ch1
DE-L229
DE-D275
DE-Bn3
DE-Brt1
DE-Zwi2
DE-D161
imprint Springer Science and Business Media LLC, 2000
imprint_str_mv Springer Science and Business Media LLC, 2000
issn 1469-221X
1469-3178
issn_str_mv 1469-221X
1469-3178
language English
mega_collection Springer Science and Business Media LLC (CrossRef)
match_str braun2000the37aprojectionmapoftheglycerolfacilitatorglpfavariantoftheaquaporintetramer
publishDateSort 2000
publisher Springer Science and Business Media LLC
recordtype ai
record_format ai
series EMBO reports
source_id 49
title The 3.7 Å projection map of the glycerol facilitator GlpF: a variant of the aquaporin tetramer
title_unstemmed The 3.7 Å projection map of the glycerol facilitator GlpF: a variant of the aquaporin tetramer
title_full The 3.7 Å projection map of the glycerol facilitator GlpF: a variant of the aquaporin tetramer
title_fullStr The 3.7 Å projection map of the glycerol facilitator GlpF: a variant of the aquaporin tetramer
title_full_unstemmed The 3.7 Å projection map of the glycerol facilitator GlpF: a variant of the aquaporin tetramer
title_short The 3.7 Å projection map of the glycerol facilitator GlpF: a variant of the aquaporin tetramer
title_sort the 3.7 å projection map of the glycerol facilitator glpf: a variant of the aquaporin tetramer
topic Genetics
Molecular Biology
Biochemistry
url http://dx.doi.org/10.1093/embo-reports/kvd022
publishDate 2000
physical 183-189
description <jats:p>GlpF, the glycerol facilitator protein of <jats:italic>Escherichia coli</jats:italic>, is an archetypal member of the aquaporin superfamily. To assess its structure, recombinant histidine‐tagged protein was overexpressed, solubilized in octylglucoside and purified to homogeneity. Negative stain electron microscopy of solubilized GlpF protein revealed a tetrameric structure of ∼80 Å side length. Scanning transmission electron microscopy yielded a mass of 170 kDa, corroborating the tetrameric nature of GlpF. Reconstitution of GlpF in the presence of lipids produced highly ordered two‐dimensional crystals, which diffracted electrons to 3.6 Å resolution. Cryoelectron microscopy provided a 3.7 Å projection map exhibiting a unit cell comprised of two tetramers. In projection, GlpF is similar to AQP1, the erythrocyte water channel. However, the major density minimum within each monomer is distinctly larger in GlpF than in AQP1.</jats:p>
container_issue 2
container_start_page 183
container_title EMBO reports
container_volume 1
format_de105 Article, E-Article
format_de14 Article, E-Article
format_de15 Article, E-Article
format_de520 Article, E-Article
format_de540 Article, E-Article
format_dech1 Article, E-Article
format_ded117 Article, E-Article
format_degla1 E-Article
format_del152 Buch
format_del189 Article, E-Article
format_dezi4 Article
format_dezwi2 Article, E-Article
format_finc Article, E-Article
format_nrw Article, E-Article
_version_ 1792342391411179522
geogr_code not assigned
last_indexed 2024-03-01T16:35:03.987Z
geogr_code_person not assigned
openURL url_ver=Z39.88-2004&ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fvufind.svn.sourceforge.net%3Agenerator&rft.title=The+3.7+%C3%85+projection+map+of+the+glycerol+facilitator+GlpF%3A+a+variant+of+the+aquaporin+tetramer&rft.date=2000-08-01&genre=article&issn=1469-3178&volume=1&issue=2&spage=183&epage=189&pages=183-189&jtitle=EMBO+reports&atitle=The+3.7+%C3%85+projection+map+of+the+glycerol+facilitator+GlpF%3A+a+variant+of+the+aquaporin+tetramer&aulast=Stahlberg&aufirst=Henning&rft_id=info%3Adoi%2F10.1093%2Fembo-reports%2Fkvd022&rft.language%5B0%5D=eng
SOLR
_version_ 1792342391411179522
author Braun, Thomas, Philippsen, Ansgar, Wirtz, Sabine, Borgnia, Mario J., Agre, Peter, Kühlbrandt, Werner, Engel, Andreas, Stahlberg, Henning
author_facet Braun, Thomas, Philippsen, Ansgar, Wirtz, Sabine, Borgnia, Mario J., Agre, Peter, Kühlbrandt, Werner, Engel, Andreas, Stahlberg, Henning, Braun, Thomas, Philippsen, Ansgar, Wirtz, Sabine, Borgnia, Mario J., Agre, Peter, Kühlbrandt, Werner, Engel, Andreas, Stahlberg, Henning
author_sort braun, thomas
container_issue 2
container_start_page 183
container_title EMBO reports
container_volume 1
description <jats:p>GlpF, the glycerol facilitator protein of <jats:italic>Escherichia coli</jats:italic>, is an archetypal member of the aquaporin superfamily. To assess its structure, recombinant histidine‐tagged protein was overexpressed, solubilized in octylglucoside and purified to homogeneity. Negative stain electron microscopy of solubilized GlpF protein revealed a tetrameric structure of ∼80 Å side length. Scanning transmission electron microscopy yielded a mass of 170 kDa, corroborating the tetrameric nature of GlpF. Reconstitution of GlpF in the presence of lipids produced highly ordered two‐dimensional crystals, which diffracted electrons to 3.6 Å resolution. Cryoelectron microscopy provided a 3.7 Å projection map exhibiting a unit cell comprised of two tetramers. In projection, GlpF is similar to AQP1, the erythrocyte water channel. However, the major density minimum within each monomer is distinctly larger in GlpF than in AQP1.</jats:p>
doi_str_mv 10.1093/embo-reports/kvd022
facet_avail Online, Free
finc_class_facet Biologie, Chemie und Pharmazie
format ElectronicArticle
format_de105 Article, E-Article
format_de14 Article, E-Article
format_de15 Article, E-Article
format_de520 Article, E-Article
format_de540 Article, E-Article
format_dech1 Article, E-Article
format_ded117 Article, E-Article
format_degla1 E-Article
format_del152 Buch
format_del189 Article, E-Article
format_dezi4 Article
format_dezwi2 Article, E-Article
format_finc Article, E-Article
format_nrw Article, E-Article
geogr_code not assigned
geogr_code_person not assigned
id ai-49-aHR0cDovL2R4LmRvaS5vcmcvMTAuMTA5My9lbWJvLXJlcG9ydHMva3ZkMDIy
imprint Springer Science and Business Media LLC, 2000
imprint_str_mv Springer Science and Business Media LLC, 2000
institution DE-Zi4, DE-Gla1, DE-15, DE-Pl11, DE-Rs1, DE-14, DE-105, DE-Ch1, DE-L229, DE-D275, DE-Bn3, DE-Brt1, DE-Zwi2, DE-D161
issn 1469-221X, 1469-3178
issn_str_mv 1469-221X, 1469-3178
language English
last_indexed 2024-03-01T16:35:03.987Z
match_str braun2000the37aprojectionmapoftheglycerolfacilitatorglpfavariantoftheaquaporintetramer
mega_collection Springer Science and Business Media LLC (CrossRef)
physical 183-189
publishDate 2000
publishDateSort 2000
publisher Springer Science and Business Media LLC
record_format ai
recordtype ai
series EMBO reports
source_id 49
spelling Braun, Thomas Philippsen, Ansgar Wirtz, Sabine Borgnia, Mario J. Agre, Peter Kühlbrandt, Werner Engel, Andreas Stahlberg, Henning 1469-221X 1469-3178 Springer Science and Business Media LLC Genetics Molecular Biology Biochemistry http://dx.doi.org/10.1093/embo-reports/kvd022 <jats:p>GlpF, the glycerol facilitator protein of <jats:italic>Escherichia coli</jats:italic>, is an archetypal member of the aquaporin superfamily. To assess its structure, recombinant histidine‐tagged protein was overexpressed, solubilized in octylglucoside and purified to homogeneity. Negative stain electron microscopy of solubilized GlpF protein revealed a tetrameric structure of ∼80 Å side length. Scanning transmission electron microscopy yielded a mass of 170 kDa, corroborating the tetrameric nature of GlpF. Reconstitution of GlpF in the presence of lipids produced highly ordered two‐dimensional crystals, which diffracted electrons to 3.6 Å resolution. Cryoelectron microscopy provided a 3.7 Å projection map exhibiting a unit cell comprised of two tetramers. In projection, GlpF is similar to AQP1, the erythrocyte water channel. However, the major density minimum within each monomer is distinctly larger in GlpF than in AQP1.</jats:p> The 3.7 Å projection map of the glycerol facilitator GlpF: a variant of the aquaporin tetramer EMBO reports
spellingShingle Braun, Thomas, Philippsen, Ansgar, Wirtz, Sabine, Borgnia, Mario J., Agre, Peter, Kühlbrandt, Werner, Engel, Andreas, Stahlberg, Henning, EMBO reports, The 3.7 Å projection map of the glycerol facilitator GlpF: a variant of the aquaporin tetramer, Genetics, Molecular Biology, Biochemistry
title The 3.7 Å projection map of the glycerol facilitator GlpF: a variant of the aquaporin tetramer
title_full The 3.7 Å projection map of the glycerol facilitator GlpF: a variant of the aquaporin tetramer
title_fullStr The 3.7 Å projection map of the glycerol facilitator GlpF: a variant of the aquaporin tetramer
title_full_unstemmed The 3.7 Å projection map of the glycerol facilitator GlpF: a variant of the aquaporin tetramer
title_short The 3.7 Å projection map of the glycerol facilitator GlpF: a variant of the aquaporin tetramer
title_sort the 3.7 å projection map of the glycerol facilitator glpf: a variant of the aquaporin tetramer
title_unstemmed The 3.7 Å projection map of the glycerol facilitator GlpF: a variant of the aquaporin tetramer
topic Genetics, Molecular Biology, Biochemistry
url http://dx.doi.org/10.1093/embo-reports/kvd022