Crystal Structure of Golgi-Associated PR-1 protein
Structural analysis of the human Golgi-associated plant pathogenesis related protein GAPR-1 implicates dimerization as a regulatory mechanism
Crystallization of a Golgi-associated PR-1-related protein (GAPR-1) that localizes to lipid-enriched microdomains
MGKSASKQFHNEVLKAHNEYRQKHGVPPLKL(OCS)KNLNREAQQYSEALASTRILKHSPESSRGQ(OCS)GENLAWASY DQTGKEVADRWYSEIKNYNFQQPGFTSGTGHFTAMVWKNTKKMGVGKASASDGSSFVVARYFPAGNVVNEGFFEENVLPP KK
MGKSASKQFHNEVLKAHNEYRQKHGVPPLKLCKNLNREAQQYSEALASTRILKHSPESSRGQCGENLAWASYDQTGKEVA DRWYSEIKNYNFQQPGFTSGTGHFTAMVWKNTKKMGVGKASASDGSSFVVARYFPAGNVVNEGFFEENVLPPKK
20% (v/v) PEG 8000, 100mM Bis-Tris, 200mM magnesium acetate, pH 7, VAPOR DIFFUSION, HANGING DROP, temperature 293K
MONOMER IN ASYMMETRIC UNIT POSSIBLE DIMER IN SOLUTION (SEE CITATION)