Rotational order–disorder structure of fluorescent protein FP480
- SAIC-Frederick Inc., Basic Research Program, Argonne National Laboratory, 9700 South Cass Avenue, Argonne, IL 60439 (United States)
- Department of Anatomy and Structural Biology, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx, New York 10461 (United States)
- Synchrotron Radiation Research Section, MCL, National Cancer Institute, Argonne National Laboratory, 9700 South Cass Avenue, Argonne, IL 60439 (United States)
An analysis of the rotational order–disorder structure of fluorescent protein FP480 is presented. 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° 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.
- OSTI ID:
- 22351186
- Journal Information:
- Acta Crystallographica. Section D: Biological Crystallography, Vol. 65, Issue Pt 9; Other Information: PMCID: PMC2733879; PMID: 19690368; PUBLISHER-ID: yt5015; OAI: oai:pubmedcentral.nih.gov:2733879; Copyright (c) International Union of Crystallography 2009; Country of input: International Atomic Energy Agency (IAEA); ISSN 0907-4449
- Country of Publication:
- Denmark
- Language:
- English
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