x * 22000, recombinant His6-SUMO-tagged enzyme, SDS-PAGE
One of the two SaGMK dimers within the crystal asymmetric unit has two monomers in different conformations: an open form with a bound sulfate ion (mimicking the beta-phosphate of ATP) and a closed form with bound GMP and sulfate ion. Each monomer is bound through its P-loop to a sulfate ion.
the recombinant refolded CaVbeta2a-GK is essentially a dimer
X-ray diffraction data for EcGMPK in complex with GCV-MP were collected at 100 K from a single crystal on beamline ID23-1 (lambda = 0.980 A) at the European Synchrotron Radiation Facility (Grenoble, France), and is indexed and scaled using XDS and XSCALE to a resolution of 3.16 A. Crystals of EcGMPK GCV-MP belong to space group P41212 and are isomorphous to those of apo-EcGMPK, with 6 molecules related by D3 symmetry in the asymmetric unit. Each monomer was first divided in 3 domains corresponding to the LID, CORE and GMP-binding domains (except for subunit F whose GMP-binding domain is not visible in apo-EcGMPK), which were submitted to rigid body refinement.
2 * 24000, SDS-PAGE, gel filtration and glutaraldehyde cross-linking
1 * 20548, calculated from amino acid sequence
1 * 23000, SDS-PAGE
monomer or dimer
the recombinant and refolded CaVbeta1b-GK is a mixture of dimers and monomers