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Crystallization, data collection and phasing of black-eyed pea trypsin/chymotrypsin inhibitor in complex with bovine β-trypsin
The black‐eyed pea trypsin and chymotrypsin inhibitor (BTCI) is a Bowman–Birk‐type inhibitor from Vigna unguiculata seeds. A complex of BTCI with bovine β‐trypsin was crystallized by the hanging‐drop vapour‐diffusion method with ammonium sulfate as precipitant. Crystals belong to the orthorhombic sp...
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| Published in: | Acta crystallographica. Section D, Biological crystallography. Biological crystallography., 2003-10, Vol.59 (10), p.1828-1830 |
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| container_end_page | 1830 |
| container_issue | 10 |
| container_start_page | 1828 |
| container_title | Acta crystallographica. Section D, Biological crystallography. |
| container_volume | 59 |
| creator | Barbosa, J. A. R. G. Teles, R. C. L. Forrer, V. P. Guimarães, B. G. Medrano, F. J. Ventura, M. M. Freitas, S. M. |
| description | The black‐eyed pea trypsin and chymotrypsin inhibitor (BTCI) is a Bowman–Birk‐type inhibitor from Vigna unguiculata seeds. A complex of BTCI with bovine β‐trypsin was crystallized by the hanging‐drop vapour‐diffusion method with ammonium sulfate as precipitant. Crystals belong to the orthorhombic space group P212121, with unit‐cell parameters a = 59.3, b = 61.8, c = 80.0 Å. Diffraction data were collected to 2.36 Å resolution and were processed to give an overall Rsym of 0.137. The Matthews coefficient for one complex per asymmetric unit is 2.2 Å3 Da−1, with a corresponding solvent content of 43%. After molecular replacement and initial refinement, the model gives an Rcryst of 0.361 and an Rfree of 0.432. |
| doi_str_mv | 10.1107/S090744490301641X |
| format | article |
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A. R. G. ; Teles, R. C. L. ; Forrer, V. P. ; Guimarães, B. G. ; Medrano, F. J. ; Ventura, M. M. ; Freitas, S. M.</creator><creatorcontrib>Barbosa, J. A. R. G. ; Teles, R. C. L. ; Forrer, V. P. ; Guimarães, B. G. ; Medrano, F. J. ; Ventura, M. M. ; Freitas, S. M.</creatorcontrib><description>The black‐eyed pea trypsin and chymotrypsin inhibitor (BTCI) is a Bowman–Birk‐type inhibitor from Vigna unguiculata seeds. A complex of BTCI with bovine β‐trypsin was crystallized by the hanging‐drop vapour‐diffusion method with ammonium sulfate as precipitant. Crystals belong to the orthorhombic space group P212121, with unit‐cell parameters a = 59.3, b = 61.8, c = 80.0 Å. Diffraction data were collected to 2.36 Å resolution and were processed to give an overall Rsym of 0.137. The Matthews coefficient for one complex per asymmetric unit is 2.2 Å3 Da−1, with a corresponding solvent content of 43%. 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M.</creatorcontrib><title>Crystallization, data collection and phasing of black-eyed pea trypsin/chymotrypsin inhibitor in complex with bovine β-trypsin</title><title>Acta crystallographica. Section D, Biological crystallography.</title><addtitle>Acta Cryst. D</addtitle><description>The black‐eyed pea trypsin and chymotrypsin inhibitor (BTCI) is a Bowman–Birk‐type inhibitor from Vigna unguiculata seeds. A complex of BTCI with bovine β‐trypsin was crystallized by the hanging‐drop vapour‐diffusion method with ammonium sulfate as precipitant. Crystals belong to the orthorhombic space group P212121, with unit‐cell parameters a = 59.3, b = 61.8, c = 80.0 Å. Diffraction data were collected to 2.36 Å resolution and were processed to give an overall Rsym of 0.137. The Matthews coefficient for one complex per asymmetric unit is 2.2 Å3 Da−1, with a corresponding solvent content of 43%. After molecular replacement and initial refinement, the model gives an Rcryst of 0.361 and an Rfree of 0.432.</description><subject>Animals</subject><subject>Cattle</subject><subject>Crystallization - methods</subject><subject>Crystallography, X-Ray - methods</subject><subject>Data Collection</subject><subject>Pisum sativum - chemistry</subject><subject>Plant Proteins - chemistry</subject><subject>Protein Conformation</subject><subject>Seeds - chemistry</subject><subject>trypsin</subject><subject>Trypsin - chemistry</subject><subject>trypsin/chymotrypsin inhibitor</subject><issn>1399-0047</issn><issn>0907-4449</issn><issn>1399-0047</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2003</creationdate><recordtype>article</recordtype><recordid>eNqFkMtu1TAURS0Eog_4ACbII0aEHsd5OMOSQqnUgniWjizbOeGaOnGwc9umE_6pH8I3kXIjQGLA6LzW3jrahDxi8IwxKPfeQwVllmUVcGBFxj7fIduMV1UCkJV3_-q3yE6MXwEgTXl5n2yxLAfGUrFNvtdhiqNyzl6r0fr-KW3UqKjxzqG5XVDVN3RYqWj7L9S3VDtlzhOccN6iomOYhvm0Z1ZT55eB2n5ltR19mLvZqhscXtFLO66o9he2R_rjJlnYB-Req1zEh0vdJR9fvvhQv0qO3xwe1fvHieEiK5IGVdoUDDgWuWAVgjai5LoAgQU3Ihe6VQ1y0WieMZNpxpu2alPFsdEqh4Lvkicb3yH4b2uMo-xsNOic6tGvoyx5UTJWiRlkG9AEH2PAVg7BdipMkoG8TV3-k_qsebyYr3WHzR_FEvMMiA1waR1O_3eU-2cH9VkOvx5PNlIbR7z6LVXhXBYlL3N5-vpQvvv09qA-PXkuc_4TYYWgiw</recordid><startdate>200310</startdate><enddate>200310</enddate><creator>Barbosa, J. 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M.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Crystallization, data collection and phasing of black-eyed pea trypsin/chymotrypsin inhibitor in complex with bovine β-trypsin</atitle><jtitle>Acta crystallographica. Section D, Biological crystallography.</jtitle><addtitle>Acta Cryst. D</addtitle><date>2003-10</date><risdate>2003</risdate><volume>59</volume><issue>10</issue><spage>1828</spage><epage>1830</epage><pages>1828-1830</pages><issn>1399-0047</issn><issn>0907-4449</issn><eissn>1399-0047</eissn><abstract>The black‐eyed pea trypsin and chymotrypsin inhibitor (BTCI) is a Bowman–Birk‐type inhibitor from Vigna unguiculata seeds. A complex of BTCI with bovine β‐trypsin was crystallized by the hanging‐drop vapour‐diffusion method with ammonium sulfate as precipitant. Crystals belong to the orthorhombic space group P212121, with unit‐cell parameters a = 59.3, b = 61.8, c = 80.0 Å. Diffraction data were collected to 2.36 Å resolution and were processed to give an overall Rsym of 0.137. The Matthews coefficient for one complex per asymmetric unit is 2.2 Å3 Da−1, with a corresponding solvent content of 43%. After molecular replacement and initial refinement, the model gives an Rcryst of 0.361 and an Rfree of 0.432.</abstract><cop>5 Abbey Square, Chester, Cheshire CH1 2HU, England</cop><pub>Munksgaard International Publishers</pub><pmid>14501128</pmid><doi>10.1107/S090744490301641X</doi><tpages>3</tpages></addata></record> |
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| language | eng |
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| source | Wiley; Alma/SFX Local Collection |
| subjects | Animals Cattle Crystallization - methods Crystallography, X-Ray - methods Data Collection Pisum sativum - chemistry Plant Proteins - chemistry Protein Conformation Seeds - chemistry trypsin Trypsin - chemistry trypsin/chymotrypsin inhibitor |
| title | Crystallization, data collection and phasing of black-eyed pea trypsin/chymotrypsin inhibitor in complex with bovine β-trypsin |
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