Apo-structure of alpha2,3-sialyltransferase variant 2 from Pasteurella dagmatis

Complete Switch from Alpha2,3- to Alpha2,6-Regioselectivity in Pasteurella Dagmatis Beta-D-Galactoside Sialyltransferase by Active-Site Redesign

SKTITIYLDHASLPTLNQLMHFTKESEDKETARIFGFSRFKLPEKITEQYNNIHFVEIKNNRPTEDIFTILDQYPEKLEL
DLHLNIAHSIQLFHPILQYRFKHPDRISIKSLNLYDDGTAEYVDLEKEENKDIKSAIKKAEKQLSDYLLTGKINFDNPTL
ARYVWQSQYPVKYHFLSTEYFEKAEFLQPLKTYLAGKYQKMDWSAYEKLSPEQQTFYLKLVGFSDETKQLFHTEQTKFIF
TGTTTWEGNTDIREYYAKQQLNLLKHFTHSEGDLFIGDQYKIYFKGHPRGGDINDYILKHAKDITNIPANISFEILMMTG
LLPDKVGGVASSLYFSLPKEKISHIIFTSNKKIKNKEDALNDPYVRVMLRLGMIDKSQIIFWDSLKQL

6.7 MG/ML PROTEIN CONCENTRATION 0.1M CITRATE, 20%W/V PEG 6000, PH 5.0

APO-STRUCTURE OF ALPHA2,3-SIALYLTRANSFERASE FROM PASTEURELLA DAGMATIS

APO-STRUCTURE OF ALPHA2,3-SIALYLTRANSFERASE VARIANT 1 FROM PASTEURELLA DAGMATIS

THE STRUCTURE OF ALPHA2,3-SIALYLTRANSFERASE VARIANT 1 FROM PASTEURELLA DAGMATIS IN COMPLEX WITH THE DONOR PRODUCT CMP

THE STRUCTURE OF ALPHA2,3-SIALYLTRANSFERASE VARIANT 2 FROM PASTEURELLA DAGMATIS IN COMPLEX WITH THE DONOR PRODUCT CMP

HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. REGION AA35-40 IS FLEXIBLE U VALUES REFINED INDIVIDUALLY