Crystallization and preliminary X-ray diffraction studies of Streptococcus pyogenes plasmid pSM19035-encoded omega transcriptional repressor.
The transcriptional repressor, omega protein, from the Streptococcus pyogenes broad-host-range plasmid pSM19035 was crystallized at pH 7. 5 and 8.5 by the vapour-diffusion method using PEG 4000 as precipitant. Two crystal forms were obtained; the first belongs to the tetragonal space group P4(1)2(1)2 or P4(3)2(1)2 and the second to the hexagonal space group P6(1) or P6(5). The crystals are most likely to contain one omega protein in the asymmetric unit, with V(m) values of 3.2 and 3.5 A(3) Da(-1), respectively. The crystals diffract X-rays to 2.4 and 2.9 A resolution for the tetragonal and hexagonal systems, -respectively.
Murayama
K
K
Institut für Kristallographie, Freie Universität Berlin, Takustrasse 6, D-14195 Berlin, Germany.
de la Hoz
A B
AB
Alings
C
C
López
G
G
Orth
P
P
Alonso
J C
JC
Saenger
W
W
D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification*; D003460:Crystallization; D018360:Crystallography, X-Ray; D010957:Plasmids / Q000235:genetics; D012097:Repressor Proteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification*; D013297:Streptococcus pyogenes / Q000737:chemistry* / Q000235:genetics
D001426:Bacterial Proteins; D012097:Repressor Proteins