Crystallization and preliminary X-ray crystallographic analysis of Mirabilis antiviral protein
Mirabilis antiviral protein is a single-chain ribosome-inactivating protein purified from the tuberous root of Mirabilis jalapa L. We obtained several forms of crystals of the protein by the hanging drop vapor diffusion method, but most of these crystals were not suitable for X-ray crystallography....
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| Veröffentlicht in: | Journal of molecular biology 1992-07, Vol.226 (1), p.281-283 |
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| container_title | Journal of molecular biology |
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| creator | Miyano, Masashi Appelt, Krzystof Arita, Masatoshi Habuka, Noriyuki Kataoka, Jiro Ago, Hideo Tsuge, Hideaki Noma, Masana Ashford, Victor Xuong, Nguyen-huu |
| description | Mirabilis antiviral protein is a single-chain ribosome-inactivating protein purified from the tuberous root of
Mirabilis jalapa L. We obtained several forms of crystals of the protein by the hanging drop vapor diffusion method, but most of these crystals were not suitable for X-ray crystallography. After refining the growth conditions, crystals of Crystallographic quality were grown in 20-μl droplets of an equi-volume mixture of 1.5% (
w
v
) protein solution and a reservoir solution containing 49 to 50% (
w
v
) ammonium sulfate and 50 m
m-ammonium citrate (pH 5.4) at room temperature. Addition of 2 m
m-adenine sulfate reduced twinning and “crystal shower”. The resulting trigonal crystals diffract beyond 2.5 Å resolution using a rotating anode X-ray generator. The space group was determined to be
P3
121 or
P3
221 (
a = b = 103.9
A
̊
, c = 134.6
A
̊
, α = β = 90 °, γ = 120 °) based on their precession photography of
h0
l and
hk0 zones. There seems to be three monomers in an asymmetric unit for
V
M
= 2.51
A
̊
3/Da
. |
| doi_str_mv | 10.1016/0022-2836(92)90142-7 |
| format | Article |
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Mirabilis jalapa L. We obtained several forms of crystals of the protein by the hanging drop vapor diffusion method, but most of these crystals were not suitable for X-ray crystallography. After refining the growth conditions, crystals of Crystallographic quality were grown in 20-μl droplets of an equi-volume mixture of 1.5% (
w
v
) protein solution and a reservoir solution containing 49 to 50% (
w
v
) ammonium sulfate and 50 m
m-ammonium citrate (pH 5.4) at room temperature. Addition of 2 m
m-adenine sulfate reduced twinning and “crystal shower”. The resulting trigonal crystals diffract beyond 2.5 Å resolution using a rotating anode X-ray generator. The space group was determined to be
P3
121 or
P3
221 (
a = b = 103.9
A
̊
, c = 134.6
A
̊
, α = β = 90 °, γ = 120 °) based on their precession photography of
h0
l and
hk0 zones. There seems to be three monomers in an asymmetric unit for
V
M
= 2.51
A
̊
3/Da
.</description><identifier>ISSN: 0022-2836</identifier><identifier>EISSN: 1089-8638</identifier><identifier>DOI: 10.1016/0022-2836(92)90142-7</identifier><identifier>PMID: 1619659</identifier><identifier>CODEN: JMOBAK</identifier><language>eng</language><publisher>Oxford: Elsevier Ltd</publisher><subject>Antiviral Agents - chemistry ; binding proteins ; Biological and medical sciences ; crystal structure ; Crystalline structure ; Crystallization ; crystals ; Fundamental and applied biological sciences. Psychology ; Macromolecular Substances ; Mirabilis antiviral protein ; Mirabilis jalapa ; Molecular biophysics ; molecular conformation ; N-Glycosyl Hydrolases ; plant proteins ; Plant Proteins - chemistry ; Plants - chemistry ; Ribosome Inactivating Proteins, Type 1 ; ribosome-inactivating protein ; ribosomes ; structure ; Structure in molecular biology ; tubers ; X-Ray Diffraction</subject><ispartof>Journal of molecular biology, 1992-07, Vol.226 (1), p.281-283</ispartof><rights>1992</rights><rights>1992 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c441t-3760fbdf6e0c48ae2a864d693b777037a2adfad0387230b0e79dd1d10f2c725a3</citedby><cites>FETCH-LOGICAL-c441t-3760fbdf6e0c48ae2a864d693b777037a2adfad0387230b0e79dd1d10f2c725a3</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(92)90142-7$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3548,27922,27923,45993</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=5363185$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1619659$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Miyano, Masashi</creatorcontrib><creatorcontrib>Appelt, Krzystof</creatorcontrib><creatorcontrib>Arita, Masatoshi</creatorcontrib><creatorcontrib>Habuka, Noriyuki</creatorcontrib><creatorcontrib>Kataoka, Jiro</creatorcontrib><creatorcontrib>Ago, Hideo</creatorcontrib><creatorcontrib>Tsuge, Hideaki</creatorcontrib><creatorcontrib>Noma, Masana</creatorcontrib><creatorcontrib>Ashford, Victor</creatorcontrib><creatorcontrib>Xuong, Nguyen-huu</creatorcontrib><title>Crystallization and preliminary X-ray crystallographic analysis of Mirabilis antiviral protein</title><title>Journal of molecular biology</title><addtitle>J Mol Biol</addtitle><description>Mirabilis antiviral protein is a single-chain ribosome-inactivating protein purified from the tuberous root of
Mirabilis jalapa L. We obtained several forms of crystals of the protein by the hanging drop vapor diffusion method, but most of these crystals were not suitable for X-ray crystallography. After refining the growth conditions, crystals of Crystallographic quality were grown in 20-μl droplets of an equi-volume mixture of 1.5% (
w
v
) protein solution and a reservoir solution containing 49 to 50% (
w
v
) ammonium sulfate and 50 m
m-ammonium citrate (pH 5.4) at room temperature. Addition of 2 m
m-adenine sulfate reduced twinning and “crystal shower”. The resulting trigonal crystals diffract beyond 2.5 Å resolution using a rotating anode X-ray generator. The space group was determined to be
P3
121 or
P3
221 (
a = b = 103.9
A
̊
, c = 134.6
A
̊
, α = β = 90 °, γ = 120 °) based on their precession photography of
h0
l and
hk0 zones. There seems to be three monomers in an asymmetric unit for
V
M
= 2.51
A
̊
3/Da
.</description><subject>Antiviral Agents - chemistry</subject><subject>binding proteins</subject><subject>Biological and medical sciences</subject><subject>crystal structure</subject><subject>Crystalline structure</subject><subject>Crystallization</subject><subject>crystals</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Macromolecular Substances</subject><subject>Mirabilis antiviral protein</subject><subject>Mirabilis jalapa</subject><subject>Molecular biophysics</subject><subject>molecular conformation</subject><subject>N-Glycosyl Hydrolases</subject><subject>plant proteins</subject><subject>Plant Proteins - chemistry</subject><subject>Plants - chemistry</subject><subject>Ribosome Inactivating Proteins, Type 1</subject><subject>ribosome-inactivating protein</subject><subject>ribosomes</subject><subject>structure</subject><subject>Structure in molecular biology</subject><subject>tubers</subject><subject>X-Ray Diffraction</subject><issn>0022-2836</issn><issn>1089-8638</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1992</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkE2LFDEQhoMo6zj6DxT7IKKH1spH5-MiyLCrwooHXfBkqE7SayTTPSY9C-OvN2MP601PRVFPvVU8hDym8IoCla8BGGuZ5vKFYS8NUMFadYesKGjTasn1XbK6Re6TB6X8AICOC31GzqikRnZmRb5t8qHMmFL8hXOcxgZH3-xySHEbR8yH5mub8dC4EzVdZ9x9j65imA4llmYamo8xYx9TbXCc403tUo2Y5hDHh-TegKmER6e6JlcX518279vLT-8-bN5etk4IOrdcSRh6P8gATmgMDLUUXhreK6WAK2ToB_TAtWIcegjKeE89hYE5xTrka_J8ya13f-5Dme02FhdSwjFM-2IVB867zvwXpFLQTnNRQbGALk-l5DDYXY7basRSsEf_9ijXHuVaw-wf__XMmjw55e_7bfB_lxbhdf7sNMfiMA0ZRxfLLdZxyanuKvZ0wQacLF7nilx9ZkA5UNVJJnQl3ixEqFpvYsi2uBhGF3zMwc3WT_Hfn_4GOaurlQ</recordid><startdate>19920705</startdate><enddate>19920705</enddate><creator>Miyano, Masashi</creator><creator>Appelt, Krzystof</creator><creator>Arita, Masatoshi</creator><creator>Habuka, Noriyuki</creator><creator>Kataoka, Jiro</creator><creator>Ago, Hideo</creator><creator>Tsuge, Hideaki</creator><creator>Noma, Masana</creator><creator>Ashford, Victor</creator><creator>Xuong, Nguyen-huu</creator><general>Elsevier Ltd</general><general>Elsevier</general><scope>FBQ</scope><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>7QL</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>M81</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>19920705</creationdate><title>Crystallization and preliminary X-ray crystallographic analysis of Mirabilis antiviral protein</title><author>Miyano, Masashi ; Appelt, Krzystof ; Arita, Masatoshi ; Habuka, Noriyuki ; Kataoka, Jiro ; Ago, Hideo ; Tsuge, Hideaki ; Noma, Masana ; Ashford, Victor ; Xuong, Nguyen-huu</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c441t-3760fbdf6e0c48ae2a864d693b777037a2adfad0387230b0e79dd1d10f2c725a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1992</creationdate><topic>Antiviral Agents - chemistry</topic><topic>binding proteins</topic><topic>Biological and medical sciences</topic><topic>crystal structure</topic><topic>Crystalline structure</topic><topic>Crystallization</topic><topic>crystals</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Macromolecular Substances</topic><topic>Mirabilis antiviral protein</topic><topic>Mirabilis jalapa</topic><topic>Molecular biophysics</topic><topic>molecular conformation</topic><topic>N-Glycosyl Hydrolases</topic><topic>plant proteins</topic><topic>Plant Proteins - chemistry</topic><topic>Plants - chemistry</topic><topic>Ribosome Inactivating Proteins, Type 1</topic><topic>ribosome-inactivating protein</topic><topic>ribosomes</topic><topic>structure</topic><topic>Structure in molecular biology</topic><topic>tubers</topic><topic>X-Ray Diffraction</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Miyano, Masashi</creatorcontrib><creatorcontrib>Appelt, Krzystof</creatorcontrib><creatorcontrib>Arita, Masatoshi</creatorcontrib><creatorcontrib>Habuka, Noriyuki</creatorcontrib><creatorcontrib>Kataoka, Jiro</creatorcontrib><creatorcontrib>Ago, Hideo</creatorcontrib><creatorcontrib>Tsuge, Hideaki</creatorcontrib><creatorcontrib>Noma, Masana</creatorcontrib><creatorcontrib>Ashford, Victor</creatorcontrib><creatorcontrib>Xuong, Nguyen-huu</creatorcontrib><collection>AGRIS</collection><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>Bacteriology Abstracts (Microbiology B)</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biochemistry Abstracts 3</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of molecular biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Miyano, Masashi</au><au>Appelt, Krzystof</au><au>Arita, Masatoshi</au><au>Habuka, Noriyuki</au><au>Kataoka, Jiro</au><au>Ago, Hideo</au><au>Tsuge, Hideaki</au><au>Noma, Masana</au><au>Ashford, Victor</au><au>Xuong, Nguyen-huu</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Crystallization and preliminary X-ray crystallographic analysis of Mirabilis antiviral protein</atitle><jtitle>Journal of molecular biology</jtitle><addtitle>J Mol Biol</addtitle><date>1992-07-05</date><risdate>1992</risdate><volume>226</volume><issue>1</issue><spage>281</spage><epage>283</epage><pages>281-283</pages><issn>0022-2836</issn><eissn>1089-8638</eissn><coden>JMOBAK</coden><abstract>Mirabilis antiviral protein is a single-chain ribosome-inactivating protein purified from the tuberous root of
Mirabilis jalapa L. We obtained several forms of crystals of the protein by the hanging drop vapor diffusion method, but most of these crystals were not suitable for X-ray crystallography. After refining the growth conditions, crystals of Crystallographic quality were grown in 20-μl droplets of an equi-volume mixture of 1.5% (
w
v
) protein solution and a reservoir solution containing 49 to 50% (
w
v
) ammonium sulfate and 50 m
m-ammonium citrate (pH 5.4) at room temperature. Addition of 2 m
m-adenine sulfate reduced twinning and “crystal shower”. The resulting trigonal crystals diffract beyond 2.5 Å resolution using a rotating anode X-ray generator. The space group was determined to be
P3
121 or
P3
221 (
a = b = 103.9
A
̊
, c = 134.6
A
̊
, α = β = 90 °, γ = 120 °) based on their precession photography of
h0
l and
hk0 zones. There seems to be three monomers in an asymmetric unit for
V
M
= 2.51
A
̊
3/Da
.</abstract><cop>Oxford</cop><pub>Elsevier Ltd</pub><pmid>1619659</pmid><doi>10.1016/0022-2836(92)90142-7</doi><tpages>3</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0022-2836 |
| ispartof | Journal of molecular biology, 1992-07, Vol.226 (1), p.281-283 |
| issn | 0022-2836 1089-8638 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_73033559 |
| source | MEDLINE; ScienceDirect Journals (5 years ago - present) |
| subjects | Antiviral Agents - chemistry binding proteins Biological and medical sciences crystal structure Crystalline structure Crystallization crystals Fundamental and applied biological sciences. Psychology Macromolecular Substances Mirabilis antiviral protein Mirabilis jalapa Molecular biophysics molecular conformation N-Glycosyl Hydrolases plant proteins Plant Proteins - chemistry Plants - chemistry Ribosome Inactivating Proteins, Type 1 ribosome-inactivating protein ribosomes structure Structure in molecular biology tubers X-Ray Diffraction |
| title | Crystallization and preliminary X-ray crystallographic analysis of Mirabilis antiviral protein |
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