{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,1,14]],"date-time":"2025-01-14T05:13:43Z","timestamp":1736831623879,"version":"3.33.0"},"reference-count":29,"publisher":"International Union of Crystallography (IUCr)","issue":"11","license":[{"start":{"date-parts":[[2014,10,25]],"date-time":"2014-10-25T00:00:00Z","timestamp":1414195200000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/journals.iucr.org\/services\/copyrightpolicy.html"},{"start":{"date-parts":[[2014,10,25]],"date-time":"2014-10-25T00:00:00Z","timestamp":1414195200000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/journals.iucr.org\/services\/copyrightpolicy.html#TDM"}],"content-domain":{"domain":["iucr.org","wiley.com","iucrj.org"],"crossmark-restriction":true},"short-container-title":["Acta Crystallogr F Struct Biol Commun","Acta Crystallogr F","Acta Crystallogr F Struct Biol Cryst Commun","Acta Cryst F","Acta Cryst F Struct Biol Commun","Acta Cryst Sect F","Acta Cryst Sect F Struct Biol Commun","Acta Crystallogr Sect F","Acta Crystallogr Sect F Struct Biol Commun","Acta Crystallogr Sect F Struct Biol Cryst Commun"],"published-print":{"date-parts":[[2014,11,1]]},"abstract":"<jats:p>Snake-venom proteins form multi-component defence systems by the recruitment and rapid evolution of nonvenomous proteins and hence serve as model systems to understand the structural modifications that result in toxicity. L-Amino-acid oxidases (LAAOs) are encountered in a number of snake venoms and have been implicated in the inhibition of platelet aggregation, cytotoxicity, haemolysis, apoptosis and haemorrhage. An L-amino-acid oxidase from<jats:italic>Lachesis muta<\/jats:italic>venom has been purified and crystallized. The crystals belonged to space group<jats:italic>P<\/jats:italic>2<jats:sub>1<\/jats:sub>, with unit-cell parameters<jats:italic>a<\/jats:italic>= 66.05,<jats:italic>b<\/jats:italic>= 79.41,<jats:italic>c<\/jats:italic>= 100.52\u2005\u00c5, \u03b2 = 96.55\u00b0. 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