Ontology highlight
ABSTRACT:
SUBMITTER: Sakamoto Y
PROVIDER: S-EPMC4321477 | biostudies-literature | 2015 Feb
REPOSITORIES: biostudies-literature
Acta crystallographica. Section F, Structural biology communications 20150128 Pt 2
Dipeptidyl peptidase 11 from Porphyromonas gingivalis (PgDPP11) preferentially cleaves substrate peptides with Asp and Glu at the P1 position [NH2-P2-P1(Asp/Glu)-P1'-P2'...]. For crystallographic studies, PgDPP11 was overproduced in Escherichia coli, purified and crystallized using the hanging-drop vapour-diffusion method. X-ray diffraction data to 1.82 Å resolution were collected from an orthorhombic crystal form belonging to space group C2221, with unit-cell parameters a = 99.33, b = 103.60, c ...[more]