Crystallization and preliminary X-ray diffraction analysis of oucleoside diphosphate kinase from Myxococcus xanthus.
Nucleoside diphosphate (NDP) kinase catalyzes the transfer of the gamma-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(1)2(1)2(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 A for form I and to 2.2 A for form II.
Williams
R L
RL
Center for Advanced Biotechnology and Medicine (CABM), Rutgers University, Piscataway, NJ 08854-5638.
Muñoz-Dorado
J
J
Jacobo-Molina
A
A
Inouye
S
S
Inouye
M
M
Arnold
E
E
D003460:Crystallization; D009231:Myxococcales / Q000201:enzymology*; D009701:Nucleoside-Diphosphate Kinase / Q000737:chemistry* / Q000302:isolation & purification; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000737:chemistry / Q000302:isolation & purification; D014961:X-Ray Diffraction / Q000379:methods
D011994:Recombinant Proteins; D009701:Nucleoside-Diphosphate Kinase