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Science, ISSN 0036-8075, 12/2014, Volume 346, Issue 6214, pp. 1242 - 1246
Journal Article
Nature Methods, ISSN 1548-7091, 01/2015, Volume 12, Issue 2, p. 109
  Unlike conventional X-ray crystallography, time-resolved X-ray crystallography (TRX) can image proteins in action. TRX is generally done using the Laue... 
Crystallography, X-Ray - methods | Photoreceptors, Microbial - ultrastructure | Bacterial Proteins - ultrastructure | Proteins | Crystallography | Biology
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 6/2010, Volume 107, Issue 24, pp. 10872 - 10877
Phytochromes are a collection of dimeric photoreceptors that direct a diverse array of responses in plants and microorganisms through photoconversion between a... 
Proteins | Maps | Architecture | Photoreceptors | Dimers | Bile pigments | Dimerization | Monomers | Crystal structure | Three dimensional modeling | Signaling helix | Light signaling | Histidine kinase | HISTIDINE KINASES | BACTERIOPHYTOCHROME | light signaling | GROUND-STATE | CRYSTAL-STRUCTURE | MULTIDISCIPLINARY SCIENCES | LIGHT | dimerization | signaling helix | X-RAY-SCATTERING | ELECTRON-MICROSCOPY | histidine kinase | SIGNAL-TRANSDUCTION | CHROMOPHORE-BINDING DOMAIN | PHOTOCONVERSION | Photoreceptors, Microbial - chemistry | Phytochrome - ultrastructure | Protein Multimerization | Bacterial Proteins - chemistry | Molecular Sequence Data | Deinococcus - genetics | Light | Protein Structure, Quaternary | Deinococcus - chemistry | Protein Interaction Domains and Motifs | Binding Sites | Phytochrome - genetics | Protein Structure, Tertiary | Amino Acid Sequence | Recombinant Proteins - ultrastructure | Photoreceptors, Microbial - ultrastructure | Bacterial Proteins - genetics | Models, Molecular | Recombinant Proteins - chemistry | Recombinant Proteins - genetics | Cryoelectron Microscopy | Deinococcus - radiation effects | Photoreceptors, Microbial - genetics | Phytochrome - chemistry | Bacterial Proteins - ultrastructure | Cryoelectron microscopy | Phytochrome | Cellular signal transduction | Research | Properties | Observations | Methods | Protein binding | Handedness | Microorganisms | Microscopy | Propagation | Protein kinase | Spine | Chromophores | phytochromes | Appendages | Light effects | ROTATION | MONOMERS | BASIC BIOLOGICAL SCIENCES | ELECTRONS | DIMERIZATION | PHYTOCHROMES | DIMERS | MICROSCOPY | CONFORMATIONAL CHANGES | POLYPEPTIDES | MICROORGANISMS | GENERAL AND MISCELLANEOUS//MATHEMATICS, COMPUTING, AND INFORMATION SCIENCE | ARCHITECTURE | PHOSPHOTRANSFERASES | PROTEINS | GROUND STATES | Biological Sciences
Journal Article
Journal Article
PLoS ONE, ISSN 1932-6203, 03/2015, Volume 10, Issue 3, p. e0118415
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 7/2012, Volume 109, Issue 30, pp. 12135 - 12140
Journal Article
Biochemistry, ISSN 0006-2960, 1995, Volume 34, Issue 19, pp. 6278 - 6287
A photosensing protein directs light energy captured by its chromophore into a photocycle. The protein's structure must accommodate the photocycle and promote... 
Protein Structure, Tertiary | Amino Acid Sequence | Bacterial Proteins - chemistry | Models, Molecular | Molecular Sequence Data | Crystallography, X-Ray | Bacterial Proteins - ultrastructure | Photoreceptors, Microbial | Chromatiaceae - chemistry | Cytosol - chemistry | Rhodopsin - chemistry
Journal Article
Integrative biology : quantitative biosciences from nano to macro, ISSN 1757-9694, 01/2012, Volume 4, Issue 1, pp. 22 - 36
The ability to sense light can be considered the most fundamental and presumably the most ancient property of visual systems. This ability is the basis of... 
Euglena gracilis - physiology | Microscopy, Electron, Scanning | Euglena gracilis - ultrastructure | Photosynthesis - physiology | Locomotion - physiology | Photoreceptor Cells - physiology | Microscopy, Fluorescence
Journal Article
Science, ISSN 0036-8075, 09/2017, Volume 357, Issue 6356, p. eaan5544
Journal Article
Biophysical Journal, ISSN 0006-3495, 07/2008, Volume 95, Issue 1, pp. 312 - 321
The flavoprotein AppA from contains an N-terminal, FAD-binding BLUF photoreceptor domain. Upon illumination, the AppA BLUF domain forms a signaling state that... 
BIOPHYSICS | LIGHT PHOTORECEPTOR | TRANSCRIPTIONAL ANTIREPRESSOR | FLAVIN-BINDING PHOTORECEPTOR | PHOTOACTIVE YELLOW PROTEIN | CRYSTAL-STRUCTURES | RHODOBACTER-SPHAEROIDES |