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Ou, Zhonghui, Felts, Richard L., Reilly, Thomas J., Nix, Jay C., Tanner, John J. (2006) Crystallization of recombinantHaemophilus influenzaee(P4) acid phosphatase. Acta Crystallographica Section F Structural Biology and Crystallization Communications, 62 (5). 464-466 doi:10.1107/s1744309106012358

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Reference TypeJournal (article/letter/editorial)
TitleCrystallization of recombinantHaemophilus influenzaee(P4) acid phosphatase
JournalActa Crystallographica Section F Structural Biology and Crystallization Communications
AuthorsOu, ZhonghuiAuthor
Felts, Richard L.Author
Reilly, Thomas J.Author
Nix, Jay C.Author
Tanner, John J.Author
Year2006 (May 1)Volume62
Issue5
PublisherInternational Union of Crystallography (IUCr)
DOIdoi:10.1107/s1744309106012358Search in ResearchGate
Generate Citation Formats
Mindat Ref. ID8491159Long-form Identifiermindat:1:5:8491159:7
GUID0
Full ReferenceOu, Zhonghui, Felts, Richard L., Reilly, Thomas J., Nix, Jay C., Tanner, John J. (2006) Crystallization of recombinantHaemophilus influenzaee(P4) acid phosphatase. Acta Crystallographica Section F Structural Biology and Crystallization Communications, 62 (5). 464-466 doi:10.1107/s1744309106012358
Plain TextOu, Zhonghui, Felts, Richard L., Reilly, Thomas J., Nix, Jay C., Tanner, John J. (2006) Crystallization of recombinantHaemophilus influenzaee(P4) acid phosphatase. Acta Crystallographica Section F Structural Biology and Crystallization Communications, 62 (5). 464-466 doi:10.1107/s1744309106012358
In(2006, May) Acta Crystallographica Section F Structural Biology and Crystallization Communications Vol. 62 (5) International Union of Crystallography (IUCr)

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Felts, Richard L., Reilly, Thomas J., Calcutt, Michael J., Tanner, John J. (2006) Cloning, purification and crystallization ofBacillus anthracisclass C acid phosphatase. Acta Crystallographica Section F Structural Biology and Crystallization Communications, 62 (7). 705-708 doi:10.1107/s174430910602389x
Felts, Richard L., Reilly, Thomas J., Calcutt, Michael J., Tanner, John J. (2006) Crystallization of a newly discovered histidine acid phosphatase fromFrancisella tularensis. Acta Crystallographica Section F Structural Biology and Crystallization Communications, 62 (1). 32-35 doi:10.1107/s1744309105039813
Singh, Harkewal, Felts, Richard L., Ma, Li, Malinski, Thomas J., Calcutt, Michael J., Reilly, Thomas J., Tanner, John J. (2009) Expression, purification and crystallization of class C acid phosphatases fromFrancisella tularensisandPasteurella multocida. Acta Crystallographica Section F Structural Biology and Crystallization Communications, 65 (3). 226-231 doi:10.1107/s1744309109001511
Singh, Harkewal, Reilly, Thomas J., Calcutt, Michael J., Tanner, John J. (2011) Expression, purification and crystallization of an atypical class C acid phosphatase fromMycoplasma bovis. Acta Crystallographica Section F Structural Biology and Crystallization Communications, 67 (10). 1296-1299 doi:10.1107/s1744309111031551
White, Tommi A., Tanner, John J. (2005) Cloning, purification and crystallization ofThermus thermophilusproline dehydrogenase. Acta Crystallographica Section F Structural Biology and Crystallization Communications, 61 (8). 737-739 doi:10.1107/s1744309105019779
Cuskin, Fiona, Solovyova, Alexandra S., Lewis, Richard J., Race, Paul R. (2011) Crystallization and preliminary X-ray analysis of the bacillaene synthasetrans-acting acyltransferase PksC. Acta Crystallographica Section F Structural Biology and Crystallization Communications, 67 (4). 464-466 doi:10.1107/s1744309111003484
Page, Richard C., Xu, Zhen, Amick, Joseph, Nix, Jay C., Misra, Saurav (2012) Crystallization and preliminary X-ray crystallographic analysis of the Bag2 amino-terminal domain fromMus musculus. Acta Crystallographica Section F Structural Biology and Crystallization Communications, 68 (6). 647-651 doi:10.1107/s1744309112013267
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Einspahr, Howard, Guss, Mitchell (2006) Acta Crystallographica Section F: developments in the first year. Acta Crystallographica Section F Structural Biology and Crystallization Communications, 62 (4). 314 doi:10.1107/s1744309106010347
 
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