2.7.7.60	?	x * 25737 is predicted from sequence of c DNA	393242	
2.7.7.60	?	x * 26000, SDS-PAGE	660697	
2.7.7.60	?	x * 27712, ES-MS	-, 393239	
2.7.7.60	?	x * 29000, SDS-PAGE, x * 25472 is predicted from sequence of c DNA	393242	
2.7.7.60	?	x * 36300, calculated	676369	
2.7.7.60	dimer	2 * 25700	393241	
2.7.7.60	dimer	2 * 25700, crystal structure analysis	660578	
2.7.7.60	dimer	2 * 26000, SDS-PAGE	-, 393244	
2.7.7.60	dimer	crystal structure analysis	661089	
2.7.7.60	dimer	each subunit contains a globular core domain with an alpha/beta sturcture and and one smaller subdomain	393240	
2.7.7.60	dimer	gel filtration	-, 726274	
2.7.7.60	dimer	homodimer	-, 393240, 393241, 393244	
2.7.7.60	dimer	the beta-domains of the monomers are mainly responsible for the formation of the dimer	-, 761358	
2.7.7.60	dimer	two crystal structures of BsIspD are determined in orthorhombic crystal form with space group P212121 and P21212, named apo form I and II, respectively. In the apo form I, two molecules in the asymmetric unit are related by 2fold sysmetry and form a dimer. In the apo form II, only one molecule is retained in the asymmetric unit, the functional dimer is formed by the sysmetry operation	-, 762421	
2.7.7.60	hexamer	-	656263	
2.7.7.60	hexamer	6 * 41700, crystal structure analysis	656263	
2.7.7.60	homodimer	-	-, 692926	
2.7.7.60	monomer	sedimentation velocity experiments, both wild-type and mutant D152A	672138	
2.7.7.60	additional information	the subunit structure of BsIspD is of a compact alpha/beta fold from which a long beta-meander extended. The core of the enzyme consists of a seven beta-sheets ( beta2, beta1, beta4, beta9, beta5, beta8, beta10 ) where all strands are parallel, apart from beta8 and beta2. The beta-meander lay between antiparallel strands beta6 and beta7 and made the major contribution to the dimer interface, and the lesser contribution came from the side-chain interactions of the residues on the alpha-helix fragment at the C-terminus. BsIspD structure, overview	-, 762421