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Diffraction study of protein crystals grown in cryoloops and micromounts
Author(s) -
Berger Michael A.,
Decker Johannes H.,
Mathews Irimpan I.
Publication year - 2010
Publication title -
journal of applied crystallography
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.429
H-Index - 162
ISSN - 1600-5767
DOI - 10.1107/s0021889810040409
Subject(s) - protein crystallization , supersaturation , crystallization , automation , diffraction , tray , crystallography , drop (telecommunication) , process (computing) , crystal (programming language) , materials science , computer science , chemistry , optics , mechanical engineering , physics , chemical engineering , engineering , telecommunications , organic chemistry , programming language , operating system
Protein crystals are usually grown in hanging or sitting drops and generally get transferred to a loop or micromount for cryocooling and data collection. This paper describes a method for growing crystals on cryoloops for easier manipulation of the crystals for data collection. This study also investigates the steps for the automation of this process and describes the design of a new tray for the method. The diffraction patterns and the structures of three proteins grown by both the new method and the conventional hanging‐drop method are compared. The new setup is optimized for the automation of the crystal mounting process. Researchers could prepare nanolitre drops under ordinary laboratory conditions by growing the crystals directly in loops or micromounts. As has been pointed out before, higher levels of supersaturation can be obtained in very small volumes, and the new method may help in the exploration of additional crystallization conditions.