| dc.contributor.author | Zaitseva, Jelena | |
| dc.contributor.author | Meneely, Kathleen M. | |
| dc.contributor.author | Lamb, Audrey L. | |
| dc.date.accessioned | 2015-04-24T17:37:46Z | |
| dc.date.available | 2015-04-24T17:37:46Z | |
| dc.date.issued | 2009-09 | |
| dc.identifier.citation | Zaitseva, Jelena, Kathleen M. Meneely, and Audrey Lee Lamb. "Structure of Escherichia Coli Malate Dehydrogenase at 1.45 Å Resolution." Acta Crystallographica Section F Structural Biology and Crystallization Communications 65.9 (2009): 866-69. Wiley Oline Library. Web. 24 Apr. 2015. http://dx.doi.org/10.1107/S1744309109032217. | en_US |
| dc.identifier.uri | http://hdl.handle.net/1808/17525 | |
| dc.description | This is the publisher's version. Copyright 2009 by the International Union of Crystallography. For full text visit http://dx.doi.org/10.1107/S1744309109032217. | en_US |
| dc.description.abstract | The structure of apo malate dehydrogenase from Escherichia coli has been determined to 1.45 Å resolution. The crystals belonged to space group C2, with unit-cell parameters a = 146.0, b = 52.0, c = 168.9 Å, [beta] = 102.2°. The structure was determined with the molecular-replacement pipeline program BALBES and was refined to a final R factor of 18.6% (Rfree = 21.4%). The final model has two dimers in the asymmetric unit. In each dimer one monomer contains the active-site loop in the open conformation, whereas in the opposing monomer the active-site loop is disordered. | en_US |
| dc.publisher | International Union of Crystallography | en_US |
| dc.title | Structure of Escherichia coli malate dehydrogenase at 1.45 Å resolution | en_US |
| dc.type | Article | |
| kusw.kuauthor | Lamb, Audrey Lee | |
| kusw.kudepartment | Molecular Biosciences | en_US |
| dc.identifier.doi | 10.1107/S1744309109032217 | |
| kusw.oaversion | Scholarly/refereed, publisher version | |
| kusw.oapolicy | This item meets KU Open Access policy criteria. | |
| dc.rights.accessrights | openAccess | |
