The MinD protein from the hyperthermophilic archaeon Pyrococcus horikoshii: crystallization and preliminary X-ray analysis.
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 P2(1)3, with unit-cell parameters a = b = c = 98.5 A, and diffract to 3.0 A resolution. The asymmetric units each contain one molecule of MinD, giving a crystal volume per protein mass (V(M)) of 3.0 A(3) Da(-1) and a solvent content of 59.0%.
Sakai
N
N
Division of Biological Sciences, Graduate School of Science, Hokkaido University, Sapporo 060-0810, Japan.
Itou
H
H
Watanabe
N
N
Yao
M
M
Tanaka
I
I
D000251:Adenosine Triphosphatases / Q000737:chemistry*; D019843:Archaeal Proteins / Q000737:chemistry*; D003001:Cloning, Molecular; D003460:Crystallization; D018360:Crystallography, X-Ray; D029968:Escherichia coli Proteins; D011487:Protein Conformation; D019711:Pyrococcus / Q000737:chemistry*; D011994:Recombinant Proteins / Q000737:chemistry
D019843:Archaeal Proteins; D029968:Escherichia coli Proteins; D011994:Recombinant Proteins; D000251:Adenosine Triphosphatases; C072069:MinD protein, E coli