dc.contributor.author |
Huang, Amadeus |
|
dc.contributor.author |
Baker, Edward |
|
dc.contributor.author |
Loomes, Kerry |
|
dc.coverage.spatial |
United States |
|
dc.date.accessioned |
2022-06-16T02:40:39Z |
|
dc.date.available |
2022-06-16T02:40:39Z |
|
dc.date.issued |
2014-11 |
|
dc.identifier.citation |
(2014). Acta Crystallographica. Section F: Structural Biology Communications, 70(Pt 11), 1546-1549. |
|
dc.identifier.issn |
2053-230X |
|
dc.identifier.uri |
https://hdl.handle.net/2292/59922 |
|
dc.description.abstract |
The enzyme 4-hydroxy-2-oxoglutarate aldolase (HOGA) catalyses the retro-aldol degradation of 4-hydroxy-2-oxoglutarate to pyruvate and glyoxylate as part of the hydroxyproline catabolic pathway in mammals. Mutations in the coding region of the human HOGA gene are associated with primary hyperoxaluria type 3, a disease characterized by excessive oxalate production and ultimately stone deposition. Native HOGA was purified from bovine kidney using an improved and streamlined purification protocol from which two crystal forms were obtained using two different approaches. Vapour diffusion using PEG 3350 as a precipitant produced monoclinic crystals that belonged to space group C2 and diffracted to 3.5 Å resolution. By comparison, orthorhombic crystals belonging to space group I222 or I2₁2₁2₁ and diffracting to beyond 2.25 Å resolution were obtained using a novel microtitration protocol with ammonium sulfate. The latter crystal form displayed superior diffraction quality and was suitable for structural determination by X-ray crystallography. |
|
dc.format.medium |
Print-Electronic |
|
dc.language |
eng |
|
dc.publisher |
International Union of Crystallography (IUCr) |
|
dc.relation.ispartofseries |
Acta crystallographica. Section F, Structural biology communications |
|
dc.rights |
Items in ResearchSpace are protected by copyright, with all rights reserved, unless otherwise indicated. Previously published items are made available in accordance with the copyright policy of the publisher. |
|
dc.rights.uri |
https://researchspace.auckland.ac.nz/docs/uoa-docs/rights.htm |
|
dc.rights.uri |
https://journals.iucr.org/services/copyrightpolicy.html |
|
dc.subject |
Animals |
|
dc.subject |
Cattle |
|
dc.subject |
Oxo-Acid-Lyases |
|
dc.subject |
Crystallization |
|
dc.subject |
X-Ray Diffraction |
|
dc.subject |
4-hydroxy-2-oxoglutarate aldolase |
|
dc.subject |
Bos taurus |
|
dc.subject |
DHDPSL |
|
dc.subject |
primary hyperoxaluria |
|
dc.subject |
Urologic Diseases |
|
dc.subject |
Science & Technology |
|
dc.subject |
Life Sciences & Biomedicine |
|
dc.subject |
Physical Sciences |
|
dc.subject |
Biochemical Research Methods |
|
dc.subject |
Biochemistry & Molecular Biology |
|
dc.subject |
Biophysics |
|
dc.subject |
Crystallography |
|
dc.subject |
DIHYDRODIPICOLINATE SYNTHASE |
|
dc.subject |
BOVINE LIVER |
|
dc.subject |
2-KETO-4-HYDROXYGLUTARATE ALDOLASE |
|
dc.subject |
MYCOBACTERIUM-TUBERCULOSIS |
|
dc.subject |
PURIFICATION |
|
dc.subject |
PROTEIN |
|
dc.subject |
HYDROXYPROLINE |
|
dc.subject |
MITOCHONDRIA |
|
dc.subject |
0306 Physical Chemistry (incl. Structural) |
|
dc.subject |
03 Chemical Sciences |
|
dc.subject |
06 Biological Sciences |
|
dc.title |
Use of a novel microtitration protocol to obtain diffraction-quality crystals of 4-hydroxy-2-oxoglutarate aldolase from Bos taurus. |
|
dc.type |
Journal Article |
|
dc.identifier.doi |
10.1107/s2053230x14021463 |
|
pubs.issue |
Pt 11 |
|
pubs.begin-page |
1546 |
|
pubs.volume |
70 |
|
dc.date.updated |
2022-05-02T08:54:23Z |
|
dc.rights.holder |
Copyright: International Union of Crystallography |
en |
dc.identifier.pmid |
25372828 (pubmed) |
|
pubs.author-url |
https://www.ncbi.nlm.nih.gov/pubmed/25372828 |
|
pubs.end-page |
1549 |
|
pubs.publication-status |
Published |
|
dc.rights.accessrights |
http://purl.org/eprint/accessRights/OpenAccess |
en |
pubs.subtype |
Research Support, Non-U.S. Gov't |
|
pubs.subtype |
research-article |
|
pubs.subtype |
Journal Article |
|
pubs.elements-id |
544107 |
|
pubs.org-id |
Science |
|
pubs.org-id |
Biological Sciences |
|
pubs.org-id |
Science Research |
|
pubs.org-id |
Maurice Wilkins Centre (2010-2014) |
|
dc.identifier.eissn |
2053-230X |
|
dc.identifier.pii |
S2053230X14021463 |
|
pubs.record-created-at-source-date |
2022-05-02 |
|
pubs.online-publication-date |
2014-10-25 |
|