Crystals of β-Xylanase from Aspergillus oryzae
An endo-xylanase was isolated from the culture of fungus Aspergillus oryzae variant D5. The purified enzyme had a molecular weight of 24,000 and the isoelectric point of 3·6. Xylanase crystals were obtained from a polyethylene glycol 6000 solution by the hanging-drop method. Seeding was used for the...
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Veröffentlicht in: | Journal of molecular biology 1993-03, Vol.230 (2), p.661-663 |
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creator | Golubev, A.M. Kilimnik, A.Yu Neustroev, K.N. Pickersgill, R.W. |
description | An endo-xylanase was isolated from the culture of fungus Aspergillus oryzae variant D5. The purified enzyme had a molecular weight of 24,000 and the isoelectric point of 3·6. Xylanase crystals were obtained from a polyethylene glycol 6000 solution by the hanging-drop method. Seeding was used for the enlargement of the crystal size. Crystals belong to the monoclinic space group P21 with cell dimensions a = 54·9 Å, b = 74·5 Å, c = 50·8 Å, and β = 108·7°. Crystals diffract beyond 2·5 Å resolution. |
doi_str_mv | 10.1006/jmbi.1993.1177 |
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The purified enzyme had a molecular weight of 24,000 and the isoelectric point of 3·6. Xylanase crystals were obtained from a polyethylene glycol 6000 solution by the hanging-drop method. Seeding was used for the enlargement of the crystal size. Crystals belong to the monoclinic space group P21 with cell dimensions a = 54·9 Å, b = 74·5 Å, c = 50·8 Å, and β = 108·7°. Crystals diffract beyond 2·5 Å resolution.</description><identifier>ISSN: 0022-2836</identifier><identifier>EISSN: 1089-8638</identifier><identifier>DOI: 10.1006/jmbi.1993.1177</identifier><identifier>PMID: 8464071</identifier><language>eng</language><publisher>England: Elsevier Ltd</publisher><subject>Aspergillus oryzae ; Aspergillus oryzae - enzymology ; Crystallization ; crystals ; Endo-1,4-beta Xylanases ; fungus ; Glycoside Hydrolases - chemistry ; Glycoside Hydrolases - isolation & purification ; Glycoside Hydrolases - metabolism ; Kinetics ; Polyethylene Glycols ; xylanase</subject><ispartof>Journal of molecular biology, 1993-03, Vol.230 (2), p.661-663</ispartof><rights>1993 Academic Press</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c370t-b5d9e71adeee00a8375d92a284f485635c5e16f1a1409613729a2994bd8ff6163</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1006/jmbi.1993.1177$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>315,781,785,3551,27929,27930,46000</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8464071$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Golubev, A.M.</creatorcontrib><creatorcontrib>Kilimnik, A.Yu</creatorcontrib><creatorcontrib>Neustroev, K.N.</creatorcontrib><creatorcontrib>Pickersgill, R.W.</creatorcontrib><title>Crystals of β-Xylanase from Aspergillus oryzae</title><title>Journal of molecular biology</title><addtitle>J Mol Biol</addtitle><description>An endo-xylanase was isolated from the culture of fungus Aspergillus oryzae variant D5. The purified enzyme had a molecular weight of 24,000 and the isoelectric point of 3·6. Xylanase crystals were obtained from a polyethylene glycol 6000 solution by the hanging-drop method. Seeding was used for the enlargement of the crystal size. Crystals belong to the monoclinic space group P21 with cell dimensions a = 54·9 Å, b = 74·5 Å, c = 50·8 Å, and β = 108·7°. Crystals diffract beyond 2·5 Å resolution.</description><subject>Aspergillus oryzae</subject><subject>Aspergillus oryzae - enzymology</subject><subject>Crystallization</subject><subject>crystals</subject><subject>Endo-1,4-beta Xylanases</subject><subject>fungus</subject><subject>Glycoside Hydrolases - chemistry</subject><subject>Glycoside Hydrolases - isolation & purification</subject><subject>Glycoside Hydrolases - metabolism</subject><subject>Kinetics</subject><subject>Polyethylene Glycols</subject><subject>xylanase</subject><issn>0022-2836</issn><issn>1089-8638</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1993</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkE1Lw0AQhhdRaq1evQk5eUu6k_3MsRS_QPCi4G3ZJLOSkjR1NxHiz_KH-JtMaPEmngbmfeZleAi5BJoApXK5afIqgSxjCYBSR2QOVGexlkwfkzmlaRqnmslTchbChlIqGNczMtNccqpgTpZrP4TO1iFqXfT9Fb8Otd3agJHzbROtwg79W1XX_Zj74dPiOTlxI40Xh7kgL7c3z-v7-PHp7mG9eowLpmgX56LMUIEtEZFSq5kaF6lNNXdcC8lEIRCkAwucZhKYSjObZhnPS-2cBMkW5Hrfu_Pte4-hM00VCqzH77Dtg1FCSg5K_AuCFCnnUo1gsgcL34bg0ZmdrxrrBwPUTCrNpNJMKs2kcjy4OjT3eYPlL35wN-Z6n-Po4aNCb0JR4bbAsvJYdKZsq7-qfwAU8IGb</recordid><startdate>19930320</startdate><enddate>19930320</enddate><creator>Golubev, A.M.</creator><creator>Kilimnik, A.Yu</creator><creator>Neustroev, K.N.</creator><creator>Pickersgill, R.W.</creator><general>Elsevier Ltd</general><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>7T7</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>M7N</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>19930320</creationdate><title>Crystals of β-Xylanase from Aspergillus oryzae</title><author>Golubev, A.M. ; Kilimnik, A.Yu ; Neustroev, K.N. ; Pickersgill, R.W.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c370t-b5d9e71adeee00a8375d92a284f485635c5e16f1a1409613729a2994bd8ff6163</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1993</creationdate><topic>Aspergillus oryzae</topic><topic>Aspergillus oryzae - enzymology</topic><topic>Crystallization</topic><topic>crystals</topic><topic>Endo-1,4-beta Xylanases</topic><topic>fungus</topic><topic>Glycoside Hydrolases - chemistry</topic><topic>Glycoside Hydrolases - isolation & purification</topic><topic>Glycoside Hydrolases - metabolism</topic><topic>Kinetics</topic><topic>Polyethylene Glycols</topic><topic>xylanase</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Golubev, A.M.</creatorcontrib><creatorcontrib>Kilimnik, A.Yu</creatorcontrib><creatorcontrib>Neustroev, K.N.</creatorcontrib><creatorcontrib>Pickersgill, R.W.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</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>Golubev, A.M.</au><au>Kilimnik, A.Yu</au><au>Neustroev, K.N.</au><au>Pickersgill, R.W.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Crystals of β-Xylanase from Aspergillus oryzae</atitle><jtitle>Journal of molecular biology</jtitle><addtitle>J Mol Biol</addtitle><date>1993-03-20</date><risdate>1993</risdate><volume>230</volume><issue>2</issue><spage>661</spage><epage>663</epage><pages>661-663</pages><issn>0022-2836</issn><eissn>1089-8638</eissn><abstract>An endo-xylanase was isolated from the culture of fungus Aspergillus oryzae variant D5. The purified enzyme had a molecular weight of 24,000 and the isoelectric point of 3·6. Xylanase crystals were obtained from a polyethylene glycol 6000 solution by the hanging-drop method. Seeding was used for the enlargement of the crystal size. Crystals belong to the monoclinic space group P21 with cell dimensions a = 54·9 Å, b = 74·5 Å, c = 50·8 Å, and β = 108·7°. Crystals diffract beyond 2·5 Å resolution.</abstract><cop>England</cop><pub>Elsevier Ltd</pub><pmid>8464071</pmid><doi>10.1006/jmbi.1993.1177</doi><tpages>3</tpages></addata></record> |
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subjects | Aspergillus oryzae Aspergillus oryzae - enzymology Crystallization crystals Endo-1,4-beta Xylanases fungus Glycoside Hydrolases - chemistry Glycoside Hydrolases - isolation & purification Glycoside Hydrolases - metabolism Kinetics Polyethylene Glycols xylanase |
title | Crystals of β-Xylanase from Aspergillus oryzae |
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