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

Cornell Affiliated Author(s)

Author

A.S.M. Soliman
M. Warkentin
B. Apker
R.E. Thorne

Abstract

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. © 2011 International Union of Crystallography Printed in Singapore - all rights reserved.

Date Published

Journal

Acta Crystallographica Section D: Biological Crystallography

Volume

67

Issue

7

Number of Pages

646-656,

URL

https://www.scopus.com/inward/record.uri?eid=2-s2.0-79959544638&doi=10.1107%2fS090744491101883X&partnerID=40&md5=a66d8667ed3e1bcb454329acf926c15b

DOI

10.1107/S090744491101883X

Research Area

Group (Lab)

Robert Thorne Group

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