9D2H
Stigmatella aurantica bacteriophytochrome protein 2 (SaBphP2), photosensory core module, investigated at ESRF(EBS) ID29. Dark Structure.
Summary for 9D2H
Entry DOI | 10.2210/pdb9d2h/pdb |
Descriptor | histidine kinase, BILIVERDINE IX ALPHA, BENZAMIDINE, ... (4 entities in total) |
Functional Keywords | photoreceptor kinase, myxobacterial phytochrome, photosensory core module., signaling protein |
Biological source | Stigmatella aurantiaca |
Total number of polymer chains | 2 |
Total formula weight | 106930.42 |
Authors | Schmidt, M.,Malla, T.N. (deposition date: 2024-08-08, release date: 2025-01-15, Last modification date: 2025-01-22) |
Primary citation | Malla, T.N.,Muniyappan, S.,Menendez, D.,Ogukwe, F.,Dale, A.N.,Clayton, J.D.,Weatherall, D.D.,Karki, P.,Dangi, S.,Mandella, V.,Pacheco, A.A.,Stojkovic, E.A.,Rose, S.L.,Orlans, J.,Basu, S.,de Sanctis, D.,Schmidt, M. Exploiting fourth-generation synchrotron radiation for enzyme and photoreceptor characterization. Iucrj, 12:36-48, 2025 Cited by PubMed Abstract: The upgrade of the European Synchrotron Radiation Facility (ESRF) in Grenoble, France to an Extremely Brilliant Source (EBS) is expected to enable time-resolved synchrotron serial crystallography (SSX) experiments with sub-millisecond time resolution. ID29 is a new beamline dedicated to SSX experiments at ESRF-EBS. Here, we report experiments emerging from the initial phase of user operation at ID29. We first used microcrystals of photoactive yellow protein as a model system to exploit the potential of microsecond pulses for SSX. Subsequently, we investigated microcrystals of cytochrome c nitrite reductase (ccNiR) with microsecond X-ray pulses. CcNiR is a decaheme protein that is ideal for the investigation of radiation damage at the various heme-iron sites. Finally, we performed a proof-of-concept subsecond time-resolved SSX experiment by photoactivating microcrystals of a myxobacterial phytochrome. PubMed: 39575537DOI: 10.1107/S2052252524010868 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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