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Article: Solution of the structure of tetrameric human glucose 6-phosphate dehydrogenase by molecular replacement
Title | Solution of the structure of tetrameric human glucose 6-phosphate dehydrogenase by molecular replacement |
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Authors | |
Issue Date | 1999 |
Publisher | International Union of Crystallography. The Journal's web site is located at http://www.wiley.com/bw/editors.asp?ref=0907-4449&site=1 |
Citation | Acta Crystallographica Section D: Biological Crystallography, 1999, v. 55 n. 4, p. 826-834 How to Cite? |
Abstract | Recombinant human glucose 6-phosphate dehydrogenase (G6PD) has been crystallized and its structure solved by molecular replacement. Crystals of the natural mutant R459L grow under similar conditions in space groups P212121 and C2221 with eight or four 515-residue molecules in the asymmetric unit, respectively. A non-crystallographic 222 tetramer was found in the C2221 crystal form using a 4 A resolution data set and a dimer of the large beta + alpha domains of the Leuconostoc mesenteroides enzyme as a search model. This tetramer was the only successful search model for the P212121 crystal form using data to 3 A. Crystals of the deletion mutant DeltaG6PD grow in space group F222 with a monomer in the asymmetric unit; 2.5 A resolution data have been collected. Comparison of the packing of tetramers in the three space groups suggests that the N-terminal tail of the enzyme prevents crystallization with exact 222 molecular symmetry. |
Persistent Identifier | http://hdl.handle.net/10722/163623 |
ISSN | 2013 Impact Factor: 7.232 |
ISI Accession Number ID |
DC Field | Value | Language |
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dc.contributor.author | Au, SWN | - |
dc.contributor.author | Naylor, CE | - |
dc.contributor.author | Gover, S | - |
dc.contributor.author | Vandeputte-Rutten, L | - |
dc.contributor.author | Scopes, DA | - |
dc.contributor.author | Mason, PJ | - |
dc.contributor.author | Luzzatto, L | - |
dc.contributor.author | Lam, VMS | - |
dc.contributor.author | Adams, MJ | - |
dc.date.accessioned | 2012-09-14T02:30:54Z | - |
dc.date.available | 2012-09-14T02:30:54Z | - |
dc.date.issued | 1999 | - |
dc.identifier.citation | Acta Crystallographica Section D: Biological Crystallography, 1999, v. 55 n. 4, p. 826-834 | - |
dc.identifier.issn | 0907-4449 | - |
dc.identifier.uri | http://hdl.handle.net/10722/163623 | - |
dc.description.abstract | Recombinant human glucose 6-phosphate dehydrogenase (G6PD) has been crystallized and its structure solved by molecular replacement. Crystals of the natural mutant R459L grow under similar conditions in space groups P212121 and C2221 with eight or four 515-residue molecules in the asymmetric unit, respectively. A non-crystallographic 222 tetramer was found in the C2221 crystal form using a 4 A resolution data set and a dimer of the large beta + alpha domains of the Leuconostoc mesenteroides enzyme as a search model. This tetramer was the only successful search model for the P212121 crystal form using data to 3 A. Crystals of the deletion mutant DeltaG6PD grow in space group F222 with a monomer in the asymmetric unit; 2.5 A resolution data have been collected. Comparison of the packing of tetramers in the three space groups suggests that the N-terminal tail of the enzyme prevents crystallization with exact 222 molecular symmetry. | - |
dc.language | eng | - |
dc.publisher | International Union of Crystallography. The Journal's web site is located at http://www.wiley.com/bw/editors.asp?ref=0907-4449&site=1 | - |
dc.relation.ispartof | Acta Crystallographica Section D: Biological Crystallography | - |
dc.subject.mesh | Amino Acid Sequence | - |
dc.subject.mesh | Base Sequence | - |
dc.subject.mesh | Crystallization | - |
dc.subject.mesh | Crystallography, X-Ray | - |
dc.subject.mesh | Glucosephosphate Dehydrogenase - chemistry - genetics | - |
dc.title | Solution of the structure of tetrameric human glucose 6-phosphate dehydrogenase by molecular replacement | en_US |
dc.type | Article | en_US |
dc.identifier.email | Lam, VMS: hrmbvel@hkucc.hku.hk | - |
dc.identifier.email | Adams, MJ: margaret@biop.ox.ac.uk | - |
dc.description.nature | published_or_final_version | - |
dc.identifier.doi | 10.1107/S0907444999000827 | - |
dc.identifier.pmid | 10089300 | - |
dc.identifier.scopus | eid_2-s2.0-0033119971 | - |
dc.identifier.hkuros | 43111 | - |
dc.identifier.volume | 55 | - |
dc.identifier.issue | 4 | - |
dc.identifier.spage | 826 | - |
dc.identifier.epage | 834 | - |
dc.identifier.isi | WOS:000079855200014 | - |
dc.publisher.place | United States | - |
dc.identifier.issnl | 0907-4449 | - |