Overproduction, purification, crystallization and preliminary X-ray diffraction analysis of YopM, an essential virulence factor extruded by the plague bacterium Yersinia pestis.
A recombinant form of Yersinia pestis YopM with a C-terminal polyhistidine affinity tag has been overproduced in Escherichia coli, purified to homogeneity and crystallized using the hanging-drop vapor-diffusion technique. Several different crystal forms were obtained. The most suitable crystals for X-ray diffraction belonged to space groups P4(2)22 (unit-cell parameters a = 109.36, b = 109.36, c = 101.50 A) and C222(1) (unit-cell parameters a = 71.73, b = 121. 85, c = 189.79 A). With a synchrotron-radiation source, these crystals diffracted to 2.4 and 1.9 A resolution, respectively.
Evdokimov
A G
AG
Protein Engineering Section, National Cancer Institute - Frederick Cancer Research and Development Center, PO Box B, Frederick, MD 21702, USA.
Anderson
D E
DE
Routzahn
K M
KM
Waugh
D S
DS
D001425:Bacterial Outer Membrane Proteins / Q000096:biosynthesis / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D018360:Crystallography, X-Ray; D010930:Plague / Q000382:microbiology; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000737:chemistry / Q000302:isolation & purification; D014774:Virulence; D015010:Yersinia pestis / Q000737:chemistry*
D001425:Bacterial Outer Membrane Proteins; D011994:Recombinant Proteins; C060772:yopM protein, Yersinia