Mass: 18.015 Da / Num. of mol.: 432 / Source method: isolated from a natural source / Formula: H2O
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Details
Sequence details
IN ORDER TO IMPROVE THE CRYSTALLIZATION PROCESS THE LAST 55 AMINO ACIDS OF THE C-TERMINAL TAIL WERE ...IN ORDER TO IMPROVE THE CRYSTALLIZATION PROCESS THE LAST 55 AMINO ACIDS OF THE C-TERMINAL TAIL WERE DELETED. THE ACTIVITY OF THE TRUNCATED FORM (PCE-55) WAS SIMILAR TO THAT OF THE WILD TYPE PROTEIN.
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Experimental details
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Experiment
Experiment
Method: X-RAY DIFFRACTION / Number of used crystals: 1
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Sample preparation
Crystal
Density Matthews: 4 Å3/Da / Density % sol: 49 % Description: STRUCTURE WAS DETERMINED BY SAD USING A NO- ISOMORPHOUS GD DERIVATIVE COLLECTED ON BEAMLINE BM30A AT ESRF. THIS MODEL WAS THEN REFINED USING HIGH RESOLUTION IN- HOUSE NATIVE DATA SET.
Crystal grow
Temperature: 293 K / pH: 5.5 Details: CRYSTALS WERE OBTAINED WITH 4 MICROL OF RESERVOIR SOLUTION (17 % PEG 10000, 0.1 M BIS TRIS PH=5.5 AND 0.1 M AMMONIUM ACETATE), 1 MICROL. OF 1.5 MM N DODECYLPHOSPHORYLCHOLINE, AND 4 MICROL. ...Details: CRYSTALS WERE OBTAINED WITH 4 MICROL OF RESERVOIR SOLUTION (17 % PEG 10000, 0.1 M BIS TRIS PH=5.5 AND 0.1 M AMMONIUM ACETATE), 1 MICROL. OF 1.5 MM N DODECYLPHOSPHORYLCHOLINE, AND 4 MICROL. OF PROTEIN SOLUTION. AT 293 K, CRYSTALS REACHED MAXIMUM DIMENSIONS OF 0.1 X 0.3 X 0.3 MM3 IN 15 30 DAYS., pH 5.50