Cyrstal structure of human alpha-synuclein (32-57) fused to maltose binding protein (MBP)
The structure was published by Zhao, M., Cascio, D., Sawaya, M.R., and Eisenberg, D., in 2011 in a paper entitled "Structures of segments of alpha-synuclein fused to maltose-binding protein suggest intermediate states during amyloid formation" (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 1.302 Å and deposited in 2010.
The experimental data on which the structure is based was also deposited.
The PDB entry contains the structure of Maltose-binding periplasmic protein/alpha-synuclein chimeric protein. This molecule has the UniProt identifier P0AEX9 (MALE_ECOLI). The sample contained 397 residues which is 99% of the natural sequence. Out of 397 residues 385 were observed and are deposited in the PDB.
It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.
The molecule is most likely monomeric.
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