Crystallization of the met repressor from Escherichia coli.
The met repressor from Escherichia coli has been crystallized in space group P21, with unit cell dimensions a = 35.6 A, b = 62.6 A, c = 44.5 A, beta = 102.4 degrees and one aporepressor dimer per asymmetric unit. Preliminary X-ray diffraction photographs show measurable intensities to beyond 1.5 A resolution, and the crystal form is ideally suited to high-resolution crystallographic analysis (1 A = 0.1 nm).
Rafferty
J B
JB
Astbury Department of Biophysics, University of Leeds, U.K.
Phillips
S E
SE
Rojas
C
C
Boulot
G
G
Saint-Girons
I
I
Guillou
Y
Y
Cohen
G N
GN
D000595:Amino Acid Sequence; D001426:Bacterial Proteins; D003460:Crystallization; D004926:Escherichia coli / Q000235:genetics*; D008715:Methionine / Q000235:genetics*; D012097:Repressor Proteins; D014157:Transcription Factors
D001426:Bacterial Proteins; D012097:Repressor Proteins; D014157:Transcription Factors; D008715:Methionine