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3N0B

TM0449 mutant crystals grown in loops/micromounts

Summary for 3N0B
Entry DOI10.2210/pdb3n0b/pdb
Related3MZQ 3MZR 3N02 3N03 3N0C
DescriptorThymidylate synthase thyX, 2'-DEOXYURIDINE 5'-MONOPHOSPHATE, FLAVIN-ADENINE DINUCLEOTIDE, ... (4 entities in total)
Functional Keywordscrystals in loops, thyx, fdts, transferase
Biological sourceThermotoga maritima
Total number of polymer chains4
Total formula weight113624.74
Authors
Mathews, I.I. (deposition date: 2010-05-13, release date: 2011-05-25, Last modification date: 2023-09-06)
Primary citationBerger, M.A.,Decker, J.H.,Mathews, I.I.
Diffraction study of protein crystals grown in cryoloops and micromounts.
J.Appl.Crystallogr., 43:1513-1518, 2010
Cited by
PubMed Abstract: 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.
PubMed: 22477781
DOI: 10.1107/S0021889810040409
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.3 Å)
Structure validation

226707

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