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Stabilization of porcine pancreatic elastase crystals by glutaraldehyde cross-linking.


ABSTRACT: Elastase is a serine protease from the chymotrypsin family of enzymes with the ability to degrade elastin, an important component of connective tissues. Excessive elastin proteolysis leads to a number of pathological diseases. Porcine pancreatic elastase (PPE) is often used for drug development as a model for human leukocyte elastase (HLE), with which it shares high sequence identity. Crystals of PPE were grown overnight using sodium sulfate and sodium acetate at acidic pH. Cross-linking the crystals with glutaraldehyde was needed to resist the soaking procedure with a diethyl N-(methyl)pyridinyl-substituted oxo-?-lactam inhibitor. Crystals of PPE bound to the inhibitor belonged to the orthorhombic space group P2?2?2?, with unit-cell parameters a = 51.0, b = 58.3, c = 74.9?Å, and diffracted to 1.8?Å resolution using an in-house X-ray source.

SUBMITTER: Hofbauer S 

PROVIDER: S-EPMC4601602 | biostudies-literature | 2015 Oct

REPOSITORIES: biostudies-literature

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Stabilization of porcine pancreatic elastase crystals by glutaraldehyde cross-linking.

Hofbauer Stefan S   Brito José A JA   Mulchande Jalmira J   Nogly Przemyslaw P   Pessanha Miguel M   Moreira Rui R   Archer Margarida M  

Acta crystallographica. Section F, Structural biology communications 20150923 Pt 10


Elastase is a serine protease from the chymotrypsin family of enzymes with the ability to degrade elastin, an important component of connective tissues. Excessive elastin proteolysis leads to a number of pathological diseases. Porcine pancreatic elastase (PPE) is often used for drug development as a model for human leukocyte elastase (HLE), with which it shares high sequence identity. Crystals of PPE were grown overnight using sodium sulfate and sodium acetate at acidic pH. Cross-linking the cry  ...[more]

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