ISSN:
1399-0047
Source:
Crystallography Journals Online : IUCR Backfile Archive 1948-2001
Topics:
Chemistry and Pharmacology
,
Geosciences
,
Physics
Notes:
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 activity. This paper deals with the first crystallization and preliminary crystallographic analysis of recombinant MinD from Pyrococcus horikoshii (molecular weight 26.3 kDa) expressed in E. coli. Crystals of MinD were obtained by the hanging-drop vapour-diffusion method. MinD crystals belong to space group P213, with unit-cell parameters a = b = c = 98.5 Å, and diffract to 3.0 Å resolution. The asymmetric units each contain one molecule of MinD, giving a crystal volume per protein mass (VM) of 3.0 Å3 Da−1 and a solvent content of 59.0%.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1107/S0907444901005728
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