Structural highlights
Publication Abstract from PubMed
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.
Diffraction study of protein crystals grown in cryoloops and micromounts.,Berger MA, Decker JH, Mathews II J Appl Crystallogr. 2010 Dec 1;43(Pt 6):1513-1518. Epub 2010 Oct 20. PMID:22477781[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Berger MA, Decker JH, Mathews II. Diffraction study of protein crystals grown in cryoloops and micromounts. J Appl Crystallogr. 2010 Dec 1;43(Pt 6):1513-1518. Epub 2010 Oct 20. PMID:22477781 doi:10.1107/S0021889810040409
