Crystallization and preliminary X-ray studies on the molbindin ModG from Azotobacter vinelandii.
Crystals of the molbindin ModG (subunit Mr = 14359 Da), a cytoplasmic molybdate-binding protein from Azotobacter vinelandii, were grown by vapour diffusion. Both apo and tungstate-bound forms were crystallized and X-ray data were collected at 100 K. Apo-ModG crystallizes in space group P6322, with unit-cell dimensions a = b = 90.62, c = 79.46 A. Native data to a resolution of 2.5 A were collected from a single crystal, which showed a marked improvement in diffraction quality after annealing. Data from a single-site gold derivative were also collected at 2.7 A resolution. Crystals of the ligand-bound form of ModG belong to space group P321, with unit-cell parameters a = b = 50.57, c = 79.29 A. X-ray data to a resolution of 2.0 A were collected.
Nitrogen Fixation Laboratory, John Innes Centre, Norwich NR4 7UH, England.
C E
CE
Williams
D J
DJ
White
L
L
Delarbre
L A
LA
Mitchenall
R N
RN
Pau
D M
DM
Lawson
D016948:Azotobacter vinelandii / Q000737:chemistry*; D001426:Bacterial Proteins; D002352:Carrier Proteins / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray; D047908:Intracellular Signaling Peptides and Proteins; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000737:chemistry
D001426:Bacterial Proteins; D002352:Carrier Proteins; D047908:Intracellular Signaling Peptides and Proteins; C101049:ModG protein, Azotobacter vinelandii; D011994:Recombinant Proteins