4R6C

X-ray diffraction in temporally and spatially resolved biomolecular science: the X-ray crystal structure of hen egg white lysozyme cocrystallized with Ta6Br12 and then a crystal soaked in K2PtBr6

Summary for 4R6C

• Entry DOI: 10.2210/pdb4r6c/pdb
• Related: 4OWH
• Descriptor: Lysozyme C, HEXATANTALUM DODECABROMIDE, HEXABROMOPLATINATE(IV), ... (7 entities in total)
• Functional Keywords: ta6br12 and ptbr6, hydrolase
• Biological source: Gallus gallus (bantam,chickens)
• Cellular location: Secreted: P00698
• Total number of polymer chains: 1
• Total formula weight: 20320.55

Authors

Helliwell, J.R. (deposition date: 2014-08-24, release date: 2015-02-04, Last modification date: 2024-10-30)

Primary citation

Helliwell, J.R.,Brink, A.,Kaenket, S.,Starkey, V.L.,Tanley, S.W.
X-ray diffraction in temporally and spatially resolved biomolecular science.
Faraday Discuss, 177:429-441, 2015

PubMed Abstract: Time-resolved Laue protein crystallography at the European Synchrotron Radiation Facility (ESRF) opened up the field of sub-nanosecond protein crystal structure analyses. There are a limited number of such time-resolved studies in the literature. Why is this? The X-ray laser now gives us femtosecond (fs) duration pulses, typically 10 fs up to ∼50 fs. Their use is attractive for the fastest time-resolved protein crystallography studies. It has been proposed that single molecules could even be studied with the advantage of being able to measure X-ray diffraction from a 'crystal lattice free' single molecule, with or without temporal resolved structural changes. This is altogether very challenging R&D. So as to assist this effort we have undertaken studies of metal clusters that bind to proteins, both 'fresh' and after repeated X-ray irradiation to assess their X-ray-photo-dynamics, namely Ta6Br12, K2PtI6 and K2PtBr6 bound to a test protein, hen egg white lysozyme. These metal complexes have the major advantage of being very recognisable shapes (pseudo spherical or octahedral) and thereby offer a start to (probably very difficult) single molecule electron density map interpretations, both static and dynamic. A further approach is to investigate the X-ray laser beam diffraction strength of a well scattering nano-cluster; an example from nature being the iron containing ferritin. Electron crystallography and single particle electron microscopy imaging offers alternatives to X-ray structural studies; our structural studies of crustacyanin, a 320 kDa protein carotenoid complex, can be extended either by electron based techniques or with the X-ray laser representing a fascinating range of options. General outlook remarks concerning X-ray, electron and neutron macromolecular crystallography as well as 'NMR crystallography' conclude the article.

PubMed: 25605312
DOI: 10.1039/c4fd00166d

Experimental method

X-RAY DIFFRACTION (1.7 Å)