File Download

There are no files associated with this item.

  Links for fulltext
     (May Require Subscription)
Supplementary

Article: Expression, purification, crystallization and preliminary X-ray crystallographic analysis of the SH3 domain of human AHI1

TitleExpression, purification, crystallization and preliminary X-ray crystallographic analysis of the SH3 domain of human AHI1
Authors
Issue Date2009
PublisherWiley-Blackwell Publishing, Inc.. The Journal's web site is located at http://www3.interscience.wiley.com/journal/117982340/home
Citation
Acta Crystallographica Section F: Structural Biology And Crystallization Communications, 2009, v. 65 n. 4, p. 361-363 How to Cite?
AbstractThe SH3 domain of human AHI1 was cloned and expressed in Escherichia coli. The protein was purified by affinity and size-exclusion chromatography and was crystallized using the sitting-drop vapour-diffusion method at 293 K. A complete data set was collected to 2.5 Å resolution at 110 K. The crystal belonged to space group P41212, with unit-cell parameters a = 67.377, b = 67.377, c = 98.549 Å. © 2009 International Union of Crystallography All rights reserved.
Persistent Identifierhttp://hdl.handle.net/10722/59261
ISSN
2014 Impact Factor: 0.524
ISI Accession Number ID
Funding AgencyGrant Number
National Science Foundation of China30670457
90813033
30811120429
Guangzhou Administration of Science and Technology2007Z2-E4021
2005Z3-C7181
Guangzhou Economic and Technological Development District2007Ss-P059
National 973 Program of China2007CB914301
2006CB910202
2004CB720102
Funding Information:

This work was supported in part by funds from the National Science Foundation of China (30670457, 90813033 and 30811120429), Guangzhou Administration of Science and Technology (2007Z2-E4021 and 2005Z3-C7181), Guangzhou Economic and Technological Development District matching funds (2007Ss-P059) and the National 973 Program of China (2007CB914301, 2006CB910202 and 2004CB720102).

References

 

DC FieldValueLanguage
dc.contributor.authorShi, Zen_HK
dc.contributor.authorLiang, Nen_HK
dc.contributor.authorXu, Wen_HK
dc.contributor.authorLi, Ken_HK
dc.contributor.authorSheng, Gen_HK
dc.contributor.authorLiu, Jen_HK
dc.contributor.authorXu, Aen_HK
dc.contributor.authorLi, XJen_HK
dc.contributor.authorWu, Den_HK
dc.date.accessioned2010-05-31T03:46:26Z-
dc.date.available2010-05-31T03:46:26Z-
dc.date.issued2009en_HK
dc.identifier.citationActa Crystallographica Section F: Structural Biology And Crystallization Communications, 2009, v. 65 n. 4, p. 361-363en_HK
dc.identifier.issn1744-3091en_HK
dc.identifier.urihttp://hdl.handle.net/10722/59261-
dc.description.abstractThe SH3 domain of human AHI1 was cloned and expressed in Escherichia coli. The protein was purified by affinity and size-exclusion chromatography and was crystallized using the sitting-drop vapour-diffusion method at 293 K. A complete data set was collected to 2.5 Å resolution at 110 K. The crystal belonged to space group P41212, with unit-cell parameters a = 67.377, b = 67.377, c = 98.549 Å. © 2009 International Union of Crystallography All rights reserved.en_HK
dc.languageengen_HK
dc.publisherWiley-Blackwell Publishing, Inc.. The Journal's web site is located at http://www3.interscience.wiley.com/journal/117982340/homeen_HK
dc.relation.ispartofActa Crystallographica Section F: Structural Biology and Crystallization Communicationsen_HK
dc.subject.meshAdaptor Proteins, Signal Transducing - chemistry - isolation & purificationen_HK
dc.subject.meshAmino Acid Sequenceen_HK
dc.subject.meshChromatography, Gelen_HK
dc.subject.meshCrystallizationen_HK
dc.subject.meshCrystallography, X-Rayen_HK
dc.subject.meshHumansen_HK
dc.subject.meshLighten_HK
dc.subject.meshMolecular Sequence Dataen_HK
dc.subject.meshRecombinant Proteins - chemistryen_HK
dc.subject.meshScattering, Radiationen_HK
dc.subject.meshSequence Alignmenten_HK
dc.subject.meshsrc Homology Domainsen_HK
dc.titleExpression, purification, crystallization and preliminary X-ray crystallographic analysis of the SH3 domain of human AHI1en_HK
dc.typeArticleen_HK
dc.identifier.emailXu, A:amxu@hkucc.hku.hken_HK
dc.identifier.authorityXu, A=rp00485en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1107/S174430910900774Xen_HK
dc.identifier.pmid19342780-
dc.identifier.scopuseid_2-s2.0-64149110148en_HK
dc.identifier.hkuros157982en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-64149110148&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume65en_HK
dc.identifier.issue4en_HK
dc.identifier.spage361en_HK
dc.identifier.epage363en_HK
dc.identifier.isiWOS:000264770000011-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridShi, Z=35206931500en_HK
dc.identifier.scopusauthoridLiang, N=36940019900en_HK
dc.identifier.scopusauthoridXu, W=7404429836en_HK
dc.identifier.scopusauthoridLi, K=35205480100en_HK
dc.identifier.scopusauthoridSheng, G=13410882100en_HK
dc.identifier.scopusauthoridLiu, J=8943925800en_HK
dc.identifier.scopusauthoridXu, A=7202655409en_HK
dc.identifier.scopusauthoridLi, XJ=36012660600en_HK
dc.identifier.scopusauthoridWu, D=7404297751en_HK
dc.identifier.citeulike4206012-

Export via OAI-PMH Interface in XML Formats


OR


Export to Other Non-XML Formats