Crystallization and preliminary X-ray analysis of Escherichia coli GlnK.
The trimeric signal-transduction protein GlnK, from Escherichia coli, has been over-expressed, purified to homogeneity and crystallized. The crystals belong to space group P213 with a = 85.53 A and have two subunits in the asymmetric unit. The complex of GlnK with ATP crystallized in space group P63 with a = 57.45 and c = 54.79 A. These crystals have a single subunit in the asymmetric unit. High-quality diffraction data from crystals of GlnK and the GlnK complex have been collected to 2.0 A.
Research School of Chemistry, Australian National University, Canberra ACT 0200, Australia.
K H
KH
MacPherson
Y
Y
Xu
E
E
Cheah
P D
PD
Carr
W C
WC
van Heeswijk
H V
HV
Westerhoff
E
E
Luque
S G
SG
Vasudevan
D L
DL
Ollis
D001426:Bacterial Proteins / Q000737:chemistry* / Q000302:isolation & purification; D002352:Carrier Proteins / Q000737:chemistry* / Q000302:isolation & purification; D003460:Crystallization; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000201:enzymology*; D011487:Protein Conformation; D011993:Recombinant Fusion Proteins / Q000737:chemistry / Q000302:isolation & purification; D015398:Signal Transduction
D001426:Bacterial Proteins; D002352:Carrier Proteins; C113488:GlnK protein, Azorhizobium caulinodans; D011993:Recombinant Fusion Proteins