{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,17]],"date-time":"2026-10-17T06:55:33Z","timestamp":1792220133886,"version":"4.4.0"},"reference-count":44,"publisher":"Wiley","issue":"20","license":[{"start":{"date-parts":[[2023,12,10]],"date-time":"2023-12-10T00:00:00Z","timestamp":1702166400000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"},{"start":{"date-parts":[[2023,12,10]],"date-time":"2023-12-10T00:00:00Z","timestamp":1702166400000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/doi.wiley.com\/10.1002\/tdm_license_1.1"}],"funder":[{"DOI":"10.13039\/501100001809","name":"National Natural Science Foundation of China","doi-asserted-by":"publisher","award":["22078093"],"award-info":[{"award-number":["22078093"]}],"id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["Small"],"published-print":{"date-parts":[[2024,5]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>\n                    A rational crystallization strategy is essential to obtain high\u2010quality protein crystals, yet the established methods suffer from different limitations arising from the single regulation on either nucleation or supersaturation. Herein, a nucleation\u2010supersaturation dual\u2010driven crystallization (DDC) strategy that realizes synergistic regulation of heterogeneous nucleation sites and solution supersaturation based on dual surface and confinement effects for efficient protein crystallization is reported. This strategy relies on a p(PEGDA\u2010\n                    <jats:italic>co<\/jats:italic>\n                    \u2010DMAA) hydrogel template with pre\u2010filled NaCl under designed concentrations. Once dropping hen egg white lysozyme (HEWL) protein solution on the hydrogel, the wrinkled surface provides numerous nucleation sites, while the internal structure regulates the solution supersaturation in the crystallization region through diffusion. Finally, DDC strategy can create high\u2010quality HEWL crystals with large sizes (100\u2013300\u00a0\u00b5m), well\u2010defined morphologies (hexagon and tetragon), and a significantly accelerated nucleation time (9\u201312 times faster than that achieved using the conventional hanging drop method). It also performs well at wider protein concentrations (10\u201350\u00a0mg\u00a0mL\n                    <jats:sup>\u22121<\/jats:sup>\n                    ) and categories (e.g., achieving fast crystallization and large\u2010size crystals of trypsin), therefore demonstrating clear advantages and great potential for efficiently fabricating protein crystals desirable for diverse applications.\n                  <\/jats:p>","DOI":"10.1002\/smll.202307924","type":"journal-article","created":{"date-parts":[[2023,12,10]],"date-time":"2023-12-10T21:59:32Z","timestamp":1702245572000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":13,"title":["Nucleation\u2010Supersaturation Dual\u2010Drive Crystallization Strategy Enables Efficient Protein 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