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Title: Development of high-performance X-ray transparent crystallization plates for in situ protein crystal screening and analysis

Journal Article · · Acta Crystallographica. Section D: Biological Crystallography
;  [1];  [2]
  1. Cornell University, Ithaca, New York (United States)
  2. MiTeGen LLC, Ithaca, New York (United States)

An optically, UV and X-ray transparent crystallization plate suitable for in situ analysis has been developed. The plate uses contact line pinning rather than wells to confine the liquids. X-ray transparent crystallization plates based upon a novel drop-pinning technology provide a flexible, simple and inexpensive approach to protein crystallization and screening. The plates consist of open cells sealed top and bottom by thin optically, UV and X-ray transparent films. The plates do not need wells or depressions to contain liquids. Instead, protein drops and reservoir solution are held in place by rings with micrometre dimensions that are patterned onto the bottom film. These rings strongly pin the liquid contact lines, thereby improving drop shape and position uniformity, and thus crystallization reproducibility, and simplifying automated image analysis of drop contents. The same rings effectively pin solutions containing salts, proteins, cryoprotectants, oils, alcohols and detergents. Strong pinning by rings allows the plates to be rotated without liquid mixing to 90° for X-ray data collection or to be inverted for hanging-drop crystallization. The plates have the standard SBS format and are compatible with standard liquid-handling robots.

OSTI ID:
22351237
Journal Information:
Acta Crystallographica. Section D: Biological Crystallography, Vol. 67, Issue Pt 7; Other Information: PMCID: PMC3121300; PMID: 21697603; PUBLISHER-ID: bw5396; OAI: oai:pubmedcentral.nih.gov:3121300; Copyright (c) International Union of Crystallography 2011; Country of input: International Atomic Energy Agency (IAEA); ISSN 0907-4449
Country of Publication:
Denmark
Language:
English