{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,21]],"date-time":"2026-10-21T13:40:34Z","timestamp":1792590034275,"version":"4.5.0"},"reference-count":0,"publisher":"The Scientific and Technological Research Council of Turkey (TUBITAK-ULAKBIM) - DIGITAL COMMONS JOURNALS","issue":"1","license":[{"start":{"date-parts":[[2026,2,25]],"date-time":"2026-02-25T00:00:00Z","timestamp":1771977600000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Turkish Journal of Chemistry"],"abstract":"<jats:p>Abelson-1 (ABL-1) is a nonreceptor tyrosine kinase that plays essential roles in various cellular processes, including\u00a0proliferation, survival, differentiation and its kinase activity is tightly regulated. The dysregulated ABL-1 kinase activity is linked to\u00a0disease pathogenesis like Chronic Myeloid Leukemia (CML), where the BCR::ABL-1 fusion oncoprotein drives oncogenic signaling. Due to its central role in CML pathogenesis, understanding the structure of ABL-1 is crucial for the effective management of the disease\u00a0and drug development studies. This study focuses on optimizing the expression, purification and crystallization of the recombinant\u00a0human ABL-1 kinase domain for its structural analysis via X-ray crystallography and structure-based drug screening applications. The\u00a0human ABL-1 kinase domain, fused with a SUMO-tag, was expressed in Escherichia coli Rosetta2 BL21 using the pET28(a)+ expression vector. The ABL-1 aggregates seen under native culture conditions were successfully solubilized by the mild ionic detergent sarkosyl.\u00a0After obtaining soluble expression of the protein, Ni-NTA affinity chromatography was performed and high yield of purified ABL-1 was\u00a0obtained. The 6X-His-SUMO-tag of purified ABL1 was cleaved by ULP1 protease. The recombinant ABL-1 was subsequently used in\u00a0crystallization trials to enlighten structural features of ABL-1 that could guide the development of novel therapeutics and drug screening platforms targeting ABL-1 in CML.<\/jats:p>","DOI":"10.55730\/1300-0527.3776","type":"journal-article","created":{"date-parts":[[2026,3,1]],"date-time":"2026-03-01T20:53:41Z","timestamp":1772398421000},"page":"12-20","source":"Crossref","is-referenced-by-count":1,"title":["Expression, purification, and crystallization of recombinant human ABL-1 kinase for X-ray crystallography"],"prefix":"10.55730","volume":"50","author":[{"given":"AY\u00c7A","family":"\u0130RG\u0130T","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"HAL\u0130L\u0130BRAH\u0130M","family":"\u00c7\u0130FT\u00c7\u0130","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"HASAN","family":"DEM\u0130RC\u0130","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"34691","published-online":{"date-parts":[[2026,2,25]]},"container-title":["Turkish Journal of Chemistry"],"original-title":[],"language":"en","deposited":{"date-parts":[[2026,10,21]],"date-time":"2026-10-21T12:53:19Z","timestamp":1792587199000},"score":1,"resource":{"primary":{"URL":"https:\/\/journals.tubitak.gov.tr\/chem\/vol50\/iss1\/3"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,2,25]]},"references-count":0,"journal-issue":{"issue":"1","published-online":{"date-parts":[[2026,2,25]]}},"URL":"https:\/\/doi.org\/10.55730\/1300-0527.3776","relation":{},"ISSN":["1300-0527"],"issn-type":[{"value":"1300-0527","type":"electronic"}],"subject":[],"published":{"date-parts":[[2026,2,25]]}}}