Crystallization and preliminary X-ray crystallographic studies of response regulator for cyanobacterial phytochrome, Rcp1.
The key response-regulator gene of light regulation, rcp1, from Synechocystis sp. has been overexpressed, purified and subsequently crystallized using ammonium sulfate as a precipitant in forms suitable for X-ray crystallographic studies. A native data set was collected to a resolution of 2.5 A at cryogenic temperature. The crystals belong to the hexagonal space group P6(3), with unit-cell parameters a = b = 89.04 (5), c = 60.29 (3) A. The Matthews parameter suggests that Rcp1 crystallizes with two molecules per asymmetric unit.
Im
Y J
YJ
Department of Life Science, Kwangju Institute of Science and Technology, Kwangju 500-712, South Korea.
Park
C M
CM
Kim
J I
JI
Yang
S S
SS
Kang
J G
JG
Rho
S H
SH
Kim
J I
JI
Song
W K
WK
Song
P S
PS
Eom
S H
SH
D000595:Amino Acid Sequence; D001426:Bacterial Proteins; D003460:Crystallization; D018360:Crystallography, X-Ray; D000458:Cyanobacteria / Q000737:chemistry*; D008969:Molecular Sequence Data; D011506:Proteins / Q000737:chemistry*; D017386:Sequence Homology, Amino Acid
D001426:Bacterial Proteins; D011506:Proteins; C107945:Rcp1 protein, Synechocystis