Crystallization and X-ray diffraction measurements on recombinant molbindin, MopII, from Clostridium pasteurianum.
Clostridium pasteurianum carries three genes termed mopI, II and III encoding three molbindin isoforms, one of which has been cloned, the gene product expressed in high yield and crystallized using the hanging-drop vapour-diffusion method. Well ordered monoclinic crystals in two different crystal forms, both with space group C2, were obtained in the presence and absence of Na(2)MoO(4) and Na(2)WO(4). Ligand-bound MopII crystallized with polyethylene glycol (PEG) 400 as a precipitant, whereas apo MopII required PEG 6000. High-resolution diffraction data were collected for ligand-bound MopII structures using synchrotron radiation to 1.8 and 1.6 A resolution for the molybdate and tungstate complexes, respectively. Data were collected on apoMopII crystals to a resolution of 1.8 A in-house.
Harrison
J A
JA
School of Life Sciences, The Wellcome Trust Biocentre, University of Dundee, Dundee DD1 5EH, Scotland.
Schüttelkopf
A W
AW
Boxer
D H
DH
Hunter
W N
WN
D001426:Bacterial Proteins / Q000737:chemistry*; D002352:Carrier Proteins / Q000737:chemistry*; D003001:Cloning, Molecular; D003013:Clostridium / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000737:chemistry
D001426:Bacterial Proteins; D002352:Carrier Proteins; D011994:Recombinant Proteins; C050771:mopI protein, Clostridium pasteurianum