Crystallization and preliminary X-ray characterization of D-3-hydroxybutyrate dehydrogenase from Pseudomonas fragi

4Citations
Citations of this article
7Readers
Mendeley users who have this article in their library.
Get full text

Abstract

A recombinant form of d-3-hydroxybutyrate dehydrogenase (EC 1.1.1.30) from Pseudomonas fragi has been crystallized by the hanging-drop method using PEG 3000 as a precipitating agent. The crystals belong to the orthorhombic group P21212, with unit-cell parameters a = 64.3, b = 99.0, c = 110.2 Å. The crystals are most likely to contain two tetrameric subunits in the asymmetric unit, with a VM value of 3.29 Å3 Da-1. Diffraction data were collected to a 2.0 Å resolution using synchrotron radiation at the BL6A station of the Photon Factory. © 2005 International Union of Crystallography All rights reserved.

Cite

CITATION STYLE

APA

Nakajima, Y., Ito, K., Ichihara, E., Ogawa, K., Egawa, T., Xu, Y., & Yoshimoto, T. (2005). Crystallization and preliminary X-ray characterization of D-3-hydroxybutyrate dehydrogenase from Pseudomonas fragi. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 61(1), 36–38. https://doi.org/10.1107/S1744309104024741

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free