Stabilization of porcine pancreatic elastase crystals by glutaraldehyde cross‐linking. Issue 10 (1st October 2015)

• Record Type: Journal Article
• Authors: Hofbauer, Stefan; Brito, José A.; Mulchande, Jalmira; Nogly, Przemyslaw; Pessanha, Miguel; Moreira, Rui; Archer, Margarida
• Is Part Of: Acta crystallographica. Volume 71:Issue 10(2015:Oct.)
• Page Start: 1346
• Page End: 1351
• Publication Date: 2015-10-01
• Subjects: Crystallography -- Periodicals; Crystals -- Periodicals; 548
• DOI: 10.1107/S2053230X15017045
• Languages: English
• ISSNs: 2053-230X

Abstract

<abstract abstract-type="main" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p>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 <italic>N</italic>‐(methyl)pyridinyl‐substituted oxo‐β‐lactam inhibitor. Crystals of PPE bound to the inhibitor belonged to the orthorhombic space group <italic>P</italic>2₁2₁2₁, with unit‐cell parameters <italic>a</italic> = 51.0, <italic>b</italic> = 58.3, <italic>c</italic> = 74.9 Å, and diffracted to 1.8 Å resolution using an in‐house X‐ray source.</p> </abstract>