Crystal structure of LamA_E269S from Z. galactanivorans in complex with laminaritriose and laminaritetraose

The Beta-Glucanase Zglama from Zobellia Galactanivorans Evolved a Bent Active Site Adapted for Efficient Degradation of Algal Laminarin

BGC B 402 HAS WRONG CHIRALITY AT ATOM C1

GERMAN COLLECTION OF MICROORGANISMS (DSM) AND IN HOUSE AT ROSCOFF COLLECTION

100 MM MIB PH 4.0, 19% PEG1500, HANGING DROP AT 20 DEGREES CELSIUS MIXING 2 MICROL OF PROTEIN (13.7 MG/ML SUPPLEMENTED WITH 5 MM PURIFIED LAMINARIHEXAOSE) WITH 1 MICROL OF RESERVOIR SOLUTION

CRYSTAL STRUCTURE OF LAMA_E269S FROM ZOBELLIA GALACTANIVORANS IN COMPLEX WITH A TRISACCHARIDE OF 1,3 -1,4-BETA-D-GLUCAN.

CRYSTAL STRUCTURE OF OF LAMACAT FROM ZOBELLIA GALACTANIVORANS

THE CONSTRUCTION CONTAINS THE CATALYTIC MODULE ONLY. THE N- TERMINAL PKD MODULE HAS NOT BEEN CLONED. THE CATALYTIC GLUTAMATE E269 HAS BEEN REPLACED BY A SERINE TO INACTIVATE THE ENZYME.

HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT U VALUES, WITH TLS ADDED

ENDO-1,3-BETA-GLUCANASE, FAMILY GH16 (E.C.3.2.1.39)

HYDROLASE, MARINE LAMINARINASE, FAMILY GH16 GLYCOSIDE HYDROLASE