Source:http://linkedlifedata.com/resource/pubmed/id/15039580
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
Pt 4
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pubmed:dateCreated |
2004-3-24
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pubmed:abstractText |
The archaebacterial-type asparagine synthetase A from Pyrococcus abyssi (AS-AR), which is related to asparaginyl-tRNA synthetase, was crystallized in two different conditions using the hanging-drop vapour-diffusion method. Crystals belonging to space group C2 with unit-cell parameters a = 103.6, b = 43.3, c = 121.5 A, beta = 112.6 degrees and one dimer per asymmetric unit were obtained in the presence of 2-propanol and PEG 4000 at pH 5.6. Another crystal form was obtained in the presence of dioxan and belongs to the monoclinic space group P2(1), with unit-cell parameters a = 96.8, b = 103.9, c = 98.4 A, beta = 107.5 degrees and two dimers per asymmetric unit. Two different native diffraction data sets were collected to 2.3 and 3.0 A resolution using synchrotron radiation and cryocooling for crystals belonging to space groups C2 and P2(1), respectively.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Archaeal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Aspartate-Ammonia Ligase,
http://linkedlifedata.com/resource/pubmed/chemical/Aspartate-tRNA Ligase,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Transfer, Amino Acyl,
http://linkedlifedata.com/resource/pubmed/chemical/asparaginyl-tRNA synthetase
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0907-4449
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
60
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
767-9
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pubmed:dateRevised |
2007-7-24
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pubmed:meshHeading |
pubmed-meshheading:15039580-Archaeal Proteins,
pubmed-meshheading:15039580-Aspartate-Ammonia Ligase,
pubmed-meshheading:15039580-Aspartate-tRNA Ligase,
pubmed-meshheading:15039580-Cloning, Molecular,
pubmed-meshheading:15039580-Crystallization,
pubmed-meshheading:15039580-Crystallography, X-Ray,
pubmed-meshheading:15039580-Pyrococcus abyssi,
pubmed-meshheading:15039580-RNA, Transfer, Amino Acyl
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pubmed:year |
2004
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pubmed:articleTitle |
Crystallization and preliminary X-ray diffraction data of an archaeal asparagine synthetase related to asparaginyl-tRNA synthetase.
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pubmed:affiliation |
Département 'Mécanismes et Macromolécules de la Synthèse Protéique et Cristallogenèse', UPR 9002, Institut de Biologie Moléculaire et Cellulaire du CNRS, 15 Rue René Descartes, F--67084 Strasbourg CEDEX, France.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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