Structural highlights
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
In the last decade, advances in instrumentation and software development have made crystallography a powerful tool in structural biology. Using this method, structural information can now be acquired from pathological crystals that would have been abandoned in earlier times. In this paper, the order-disorder (OD) structure of fluorescent protein FP480 is discussed. The structure is composed of tetramers with 222 symmetry incorporated into the lattice in two different ways, namely rotated 90 degrees with respect to each other around the crystal c axis, with tetramer axes coincident with crystallographic twofold axes. The random distribution of alternatively oriented tetramers in the crystal creates a rotational OD structure with statistically averaged I422 symmetry, although the presence of very weak and diffuse additional reflections suggests that the randomness is only approximate.
Rotational order-disorder structure of fluorescent protein FP480.,Pletnev S, Morozova KS, Verkhusha VV, Dauter Z Acta Crystallogr D Biol Crystallogr. 2009 Sep;65(Pt 9):906-12. Epub 2009, Aug 6. PMID:19690368[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Pletnev S, Morozova KS, Verkhusha VV, Dauter Z. Rotational order-disorder structure of fluorescent protein FP480. Acta Crystallogr D Biol Crystallogr. 2009 Sep;65(Pt 9):906-12. Epub 2009, Aug 6. PMID:19690368 doi:10.1107/S0907444909020927