Crystallographic analysis of acrosomal bundle from Limulus sperm
The acrosomal process of Limulus sperm contains a bundle of filaments composed of actin and a 102 kDa protein in a 1:1 molar ratio. The structure of the bundle in true discharge was investigated by electron cryomicroscopy, X-ray scattering and crystallographic image analysis. A bundle can be charact...
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| Veröffentlicht in: | Journal of molecular biology 1991-09, Vol.221 (2), p.711-725 |
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| creator | Schmid, M.F. Matsudaira, P. Jeng, T.-W. Jakana, J. Towns-Andrews, E. Bordas, J. Chiu, W. |
| description | The acrosomal process of
Limulus sperm contains a bundle of filaments composed of actin and a 102 kDa protein in a 1:1 molar ratio. The structure of the bundle in true discharge was investigated by electron cryomicroscopy, X-ray scattering and crystallographic image analysis. A bundle can be characterized as a quasi-crystal with continuously varying views along the bundle axis. Each segment of the bundle is found to obey the symmetry of space group
P1, with
a = b = 147
A
̊
, c = 762
A
̊
, α = 90°, β = 90·6°, γ = 120°
. A unit cell contains a helical repeat of the filament with a selection rule following that of an actin filament. A 24 Å projection map based on the
h0l view was reconstructed after averaging 5300 unit cells from six electron images. Filaments in this projection are well separated and clearly display a 2
1 screw symmetry. This screw symmetry results from the helical parameters of the bundle filament and is found to be a non-crystallographic symmetry element present in the unit cell. Our structural analysis has led to the proposal that the assembly of a stable bundle with a defined maximum diameter can be controlled by the crystallographic packing of the twisted filaments. |
| doi_str_mv | 10.1016/0022-2836(91)80082-6 |
| format | Article |
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Limulus sperm contains a bundle of filaments composed of actin and a 102 kDa protein in a 1:1 molar ratio. The structure of the bundle in true discharge was investigated by electron cryomicroscopy, X-ray scattering and crystallographic image analysis. A bundle can be characterized as a quasi-crystal with continuously varying views along the bundle axis. Each segment of the bundle is found to obey the symmetry of space group
P1, with
a = b = 147
A
̊
, c = 762
A
̊
, α = 90°, β = 90·6°, γ = 120°
. A unit cell contains a helical repeat of the filament with a selection rule following that of an actin filament. A 24 Å projection map based on the
h0l view was reconstructed after averaging 5300 unit cells from six electron images. Filaments in this projection are well separated and clearly display a 2
1 screw symmetry. This screw symmetry results from the helical parameters of the bundle filament and is found to be a non-crystallographic symmetry element present in the unit cell. Our structural analysis has led to the proposal that the assembly of a stable bundle with a defined maximum diameter can be controlled by the crystallographic packing of the twisted filaments.</description><identifier>ISSN: 0022-2836</identifier><identifier>EISSN: 1089-8638</identifier><identifier>DOI: 10.1016/0022-2836(91)80082-6</identifier><identifier>PMID: 1920441</identifier><identifier>CODEN: JMOBAK</identifier><language>eng</language><publisher>Oxford: Elsevier Ltd</publisher><subject>acrosomal process ; Acrosome - chemistry ; Acrosome - ultrastructure ; actin ; Actins - chemistry ; Actins - isolation & purification ; Actins - ultrastructure ; Animals ; Biological and medical sciences ; Crystalline structure ; electron cryomicroscopy ; Freeze Fracturing ; Fundamental and applied biological sciences. Psychology ; Horseshoe Crabs - chemistry ; Horseshoe Crabs - ultrastructure ; Image Processing, Computer-Assisted ; Male ; Molecular biophysics ; Molecular Weight ; Peptides - chemistry ; Peptides - isolation & purification ; Structure in molecular biology ; X-Ray Diffraction</subject><ispartof>Journal of molecular biology, 1991-09, Vol.221 (2), p.711-725</ispartof><rights>1991</rights><rights>1992 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c386t-e181f47cf610f647a7fd83907b2185c89786f1db61d4faa04130b5e7cfa858893</citedby><cites>FETCH-LOGICAL-c386t-e181f47cf610f647a7fd83907b2185c89786f1db61d4faa04130b5e7cfa858893</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/0022-2836(91)80082-6$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>315,781,785,3551,27929,27930,46000</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=4975053$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1920441$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Schmid, M.F.</creatorcontrib><creatorcontrib>Matsudaira, P.</creatorcontrib><creatorcontrib>Jeng, T.-W.</creatorcontrib><creatorcontrib>Jakana, J.</creatorcontrib><creatorcontrib>Towns-Andrews, E.</creatorcontrib><creatorcontrib>Bordas, J.</creatorcontrib><creatorcontrib>Chiu, W.</creatorcontrib><title>Crystallographic analysis of acrosomal bundle from Limulus sperm</title><title>Journal of molecular biology</title><addtitle>J Mol Biol</addtitle><description>The acrosomal process of
Limulus sperm contains a bundle of filaments composed of actin and a 102 kDa protein in a 1:1 molar ratio. The structure of the bundle in true discharge was investigated by electron cryomicroscopy, X-ray scattering and crystallographic image analysis. A bundle can be characterized as a quasi-crystal with continuously varying views along the bundle axis. Each segment of the bundle is found to obey the symmetry of space group
P1, with
a = b = 147
A
̊
, c = 762
A
̊
, α = 90°, β = 90·6°, γ = 120°
. A unit cell contains a helical repeat of the filament with a selection rule following that of an actin filament. A 24 Å projection map based on the
h0l view was reconstructed after averaging 5300 unit cells from six electron images. Filaments in this projection are well separated and clearly display a 2
1 screw symmetry. This screw symmetry results from the helical parameters of the bundle filament and is found to be a non-crystallographic symmetry element present in the unit cell. Our structural analysis has led to the proposal that the assembly of a stable bundle with a defined maximum diameter can be controlled by the crystallographic packing of the twisted filaments.</description><subject>acrosomal process</subject><subject>Acrosome - chemistry</subject><subject>Acrosome - ultrastructure</subject><subject>actin</subject><subject>Actins - chemistry</subject><subject>Actins - isolation & purification</subject><subject>Actins - ultrastructure</subject><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Crystalline structure</subject><subject>electron cryomicroscopy</subject><subject>Freeze Fracturing</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Horseshoe Crabs - chemistry</subject><subject>Horseshoe Crabs - ultrastructure</subject><subject>Image Processing, Computer-Assisted</subject><subject>Male</subject><subject>Molecular biophysics</subject><subject>Molecular Weight</subject><subject>Peptides - chemistry</subject><subject>Peptides - isolation & purification</subject><subject>Structure in molecular biology</subject><subject>X-Ray Diffraction</subject><issn>0022-2836</issn><issn>1089-8638</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1991</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kEtLxDAUhYMo4_j4BwpdiOiimtum6e1GlMEXDLjRdUjTRCPpw6QV5t_bOsO4c3UX5zuHy0fICdAroMCvKU2SOMGUXxRwiZRiEvMdMgeKRYw8xV0y3yL75CCET0ppljKckRkUCWUM5uR24Vehl8617152H1ZFspFuFWyIWhNJ5dvQ1tJF5dBUTkfGt3W0tPXghhCFTvv6iOwZ6YI-3txD8vZw_7p4ipcvj8-Lu2WsUuR9rAHBsFwZDtRwlsvcVJgWNC8TwExhkSM3UJUcKmakpAxSWmZ6LEjMEIv0kJyvdzvffg069KK2QWnnZKPbIYg8gQSzDEeQrcHp9-C1EZ23tfQrAVRM4sRkRUxWRAHiV5zgY-10sz-Uta7-SmtTY362yWVQ0hkvG2XDFmNFno1yR-xmjenRxbfVXgRldaN0Zb1Wvaha-_8fP0BGiNw</recordid><startdate>19910920</startdate><enddate>19910920</enddate><creator>Schmid, M.F.</creator><creator>Matsudaira, P.</creator><creator>Jeng, T.-W.</creator><creator>Jakana, J.</creator><creator>Towns-Andrews, E.</creator><creator>Bordas, J.</creator><creator>Chiu, W.</creator><general>Elsevier Ltd</general><general>Elsevier</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>19910920</creationdate><title>Crystallographic analysis of acrosomal bundle from Limulus sperm</title><author>Schmid, M.F. ; Matsudaira, P. ; Jeng, T.-W. ; Jakana, J. ; Towns-Andrews, E. ; Bordas, J. ; Chiu, W.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c386t-e181f47cf610f647a7fd83907b2185c89786f1db61d4faa04130b5e7cfa858893</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1991</creationdate><topic>acrosomal process</topic><topic>Acrosome - chemistry</topic><topic>Acrosome - ultrastructure</topic><topic>actin</topic><topic>Actins - chemistry</topic><topic>Actins - isolation & purification</topic><topic>Actins - ultrastructure</topic><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Crystalline structure</topic><topic>electron cryomicroscopy</topic><topic>Freeze Fracturing</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Horseshoe Crabs - chemistry</topic><topic>Horseshoe Crabs - ultrastructure</topic><topic>Image Processing, Computer-Assisted</topic><topic>Male</topic><topic>Molecular biophysics</topic><topic>Molecular Weight</topic><topic>Peptides - chemistry</topic><topic>Peptides - isolation & purification</topic><topic>Structure in molecular biology</topic><topic>X-Ray Diffraction</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Schmid, M.F.</creatorcontrib><creatorcontrib>Matsudaira, P.</creatorcontrib><creatorcontrib>Jeng, T.-W.</creatorcontrib><creatorcontrib>Jakana, J.</creatorcontrib><creatorcontrib>Towns-Andrews, E.</creatorcontrib><creatorcontrib>Bordas, J.</creatorcontrib><creatorcontrib>Chiu, W.</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of molecular biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Schmid, M.F.</au><au>Matsudaira, P.</au><au>Jeng, T.-W.</au><au>Jakana, J.</au><au>Towns-Andrews, E.</au><au>Bordas, J.</au><au>Chiu, W.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Crystallographic analysis of acrosomal bundle from Limulus sperm</atitle><jtitle>Journal of molecular biology</jtitle><addtitle>J Mol Biol</addtitle><date>1991-09-20</date><risdate>1991</risdate><volume>221</volume><issue>2</issue><spage>711</spage><epage>725</epage><pages>711-725</pages><issn>0022-2836</issn><eissn>1089-8638</eissn><coden>JMOBAK</coden><abstract>The acrosomal process of
Limulus sperm contains a bundle of filaments composed of actin and a 102 kDa protein in a 1:1 molar ratio. The structure of the bundle in true discharge was investigated by electron cryomicroscopy, X-ray scattering and crystallographic image analysis. A bundle can be characterized as a quasi-crystal with continuously varying views along the bundle axis. Each segment of the bundle is found to obey the symmetry of space group
P1, with
a = b = 147
A
̊
, c = 762
A
̊
, α = 90°, β = 90·6°, γ = 120°
. A unit cell contains a helical repeat of the filament with a selection rule following that of an actin filament. A 24 Å projection map based on the
h0l view was reconstructed after averaging 5300 unit cells from six electron images. Filaments in this projection are well separated and clearly display a 2
1 screw symmetry. This screw symmetry results from the helical parameters of the bundle filament and is found to be a non-crystallographic symmetry element present in the unit cell. Our structural analysis has led to the proposal that the assembly of a stable bundle with a defined maximum diameter can be controlled by the crystallographic packing of the twisted filaments.</abstract><cop>Oxford</cop><pub>Elsevier Ltd</pub><pmid>1920441</pmid><doi>10.1016/0022-2836(91)80082-6</doi><tpages>15</tpages></addata></record> |
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| subjects | acrosomal process Acrosome - chemistry Acrosome - ultrastructure actin Actins - chemistry Actins - isolation & purification Actins - ultrastructure Animals Biological and medical sciences Crystalline structure electron cryomicroscopy Freeze Fracturing Fundamental and applied biological sciences. Psychology Horseshoe Crabs - chemistry Horseshoe Crabs - ultrastructure Image Processing, Computer-Assisted Male Molecular biophysics Molecular Weight Peptides - chemistry Peptides - isolation & purification Structure in molecular biology X-Ray Diffraction |
| title | Crystallographic analysis of acrosomal bundle from Limulus sperm |
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