Crystallization and preliminary X-ray crystallographic analysis of human nucleoside diphosphate kinase A.
Human nucleoside diphosphate kinase A catalyzes phosphoryl transfer and acts as a suppressor of metastasis. It has been crystallized using 2-methyl-2,4-pentanediol as a precipitant at 288 K. The crystal is monoclinic, belonging to the space group P2(1), with unit-cell parameters a = 74.21, b = 78.11, c = 82.29 A, beta = 101. 33 degrees. The asymmetric unit contains a homohexamer, with a corresponding crystal volume per protein mass (V(m)) of 2.27 A(3) Da(-1) and a solvent content of 46%. Native X-ray data to 2.15 A resolution have been collected using synchrotron X-rays.
Min
K
K
Department of Chemistry, College of Natural Sciences, Seoul National University, Seoul 151--742, South Korea.
Kim
S Y
SY
Song
H K
HK
Chang
C
C
Cho
S J
SJ
Moon
J
J
Yang
J K
JK
Lee
J Y
JY
Lee
K J
KJ
Suh
S W
SW
D003460:Crystallization; D018360:Crystallography, X-Ray; D006801:Humans; D046911:Macromolecular Substances; D009701:Nucleoside-Diphosphate Kinase / Q000737:chemistry* / Q000302:isolation & purification; D011994:Recombinant Proteins / Q000737:chemistry / Q000302:isolation & purification
D046911:Macromolecular Substances; D011994:Recombinant Proteins; D009701:Nucleoside-Diphosphate Kinase