Structure of monellin refined to 2.3 a resolution in the orthorhombic crystal form.
REJECTION CRITERIA DEFAULT FOR DATA COLLECTION USING XENGEN IS -3 SIGMA; THIS VALUE WAS NOT ALLOWED BY PDB DEPOSITION SOFTWARE.
5-10 MG/ML PROTEIN DISSOLVED IN 100 MM SODIUM PHOSPHATE BUFFER, PH 7.2, DIFFUSED AGAINST 20 W/V % ETHANOL. CRYSTALS UNSTABLE- CROSSLINKED WITH 0.015% GLUTARALDEHYDE FOR 1-1.5 HOURS.
PHE 1, RESIDUE PHE 1, NOTED IN SWISS-PROT P02881 AS {VARIANT...MISSING (IN 90% OF THE CHAINS)}, IS NOT VISIBLE IN THIS STRUCTURE. THE SEQUENCE OF THE LAST TWO RESIDUES OF THE B/D CHAIN HAS BEEN REMARK 999 GIVEN AS EITHER ASNGLU OR GLUASN, DEPENDING ON THE SOURCE OF THE DATA. THE SEQUENCE USED HERE WAS PREVIOUSLY REPORTED IN THE FILE 3MON, WHICH WAS UTILIZED FOR MOLECULAR REPLACEMENT. WHILE THIS SEQUENCE IS MOST LIKELY INCORRECT (SEE BELOW), IT WAS NOT MODIFIED, SINCE THE ELECTRON DENSITY IN THIS REGION WAS NOT SUFFICIENTLY GOOD TO DISTINGUISH BETWEEN THE TWO POSSIBILITIES AND THE AUTHORS PREFERRED TO REMAIN COMPATIBLE WITH THE PREVIOUS ENTRY.
INITIAL REFINEMENT PERFORMED WITH X-PLOR, FOLLOWED BY MODEL BUILDING WITH FRODO AND FURTHER REFINEMENT WITH PROLSQ (PROFFT VERSION).
SWEET-TASTING PROTEIN, ORTHORHOMBIC CRYSTALS