Abstract
Nucleoside diphosphate (NDP) kinase catalyzes the transfer of the γ-phosphate from a nucleoside triphosphate to a nucleoside diphosphate. Human and rodent forms of this enzyme have been shown to be suppressors of metastasis. Crystals that diffract X-rays to high resolution have been obtained for the recombinant
Myxococcus xanthus NDP kinase expressed in and purified from
Escherichia coli. Two crystal forms have been obtained. Both forms are orthorhombic, space group
I222 (or
I2
12
12
1) with
a = 267·1
A
̊
, b = 74·0
A
̊
and
c = 75·1
A
̊
for form I and
a = 53·5
A
̊
, b = 74·0
A
̊
and
c = 75·1
A
̊
for form II. Form I appears to have five molecules in the asymmetric unit approximately related to each other by a translation of 0·2 along the
a axis. Diffraction data have been recorded to 1·9 Å for form I and to 2·2 Å for form II.