The MinD protein from the hyperthermophilic archaeon Pyrococcus horikoshii: crystallization and preliminary X-ray analysis

Citation
N. Sakai et al., The MinD protein from the hyperthermophilic archaeon Pyrococcus horikoshii: crystallization and preliminary X-ray analysis, ACT CRYST D, 57, 2001, pp. 896-897
Citations number
16
Language
INGLESE
art.tipo
Article
Categorie Soggetti
Chemistry & Analysis
Journal title
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
ISSN journal
0907-4449 → ACNP
Volume
57
Year of publication
2001
Part
6
Pages
896 - 897
Database
ISI
SICI code
0907-4449(200106)57:<896:TMPFTH>2.0.ZU;2-A
Abstract
MinD is one of the proteins regulating cell division. MinD from Escherichia coli has been designated as a type of motor protein which has an ATPase ac tivity. This paper deals with the first crystallization and preliminary cry stallographic analysis of recombinant MinD from Pyrococcus horikoshii (mole cular weight 26.3 kDa) expressed in E. coli. Crystals of MinD were obtained by the hanging-drop vapour-iffusion method. MinD crystals belong to space group P2(1)3, with unit-cell parameters a = b = c = 98.5 Angstrom, and diff ract to 3.0 Angstrom resolution. The asymmetric units each contain one mole cule of MinD, giving a crystal volume per protein mass (VM) of 3.0 Angstrom (3) Da(-1) and a solvent content of 59.0%.