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Structure determination of oxygen-evolving photosystem II from T. vulcanus at 3.7 angstrom resolution

  • Only SPring-8

Inquiry number

SOL-0000001163

Beamline

BL41XU (Macromolecular Crystallography I)

Scientific keywords

A. Sample category biology, medicine
B. Sample category (detail) biomolecule, crystal, protein
C. Technique X-ray diffraction
D. Technique (detail) single crystal
E. Particular condition low-T (~ liquid N2)
F. Photon energy X-ray (4-40 keV)
G. Target information chemical state, molecular structure, structure analysis, function and structure, charge density

Industrial keywords

level 1---Application area environment, Pharmaceuticals
level 2---Target catalysis, drug design, process analytical technology (PAT)
level 3---Target (detail) protein, drug
level 4---Obtainable information interatomic distance, supra-molecular assemblies
level 5---Technique diffraction

Classification

A80.32 organic material, A80.50 Pharmaceuticals, M10.10 single crystal diffraction

Body text

In the initial step of photosynthesis, water molecule is splitting to an oxygen molecule and electrons needed to later steps. Photosystem II is a membrane protein complex to do this reaction.

In this case, crystal structure of oxygen-evolving photosystem II from thermophilic cyanobacteria T. vulcanus was determined at 3.7 Å resolution (Fig. 1).

Generally, most crystals of membrane protein have only weak ability to diffract X-ray. The unit cell of this crystal is large, 129.7x226.5x307.8 Å. High brilliant X-ray from undulator of BL41XU was indispensable to collect the good X-ray diffraction data.

Three-dimensional pathway of light-induced electron transfer (Fig. 2) and constitution of water-splitting Mn cluster (Fig. 3) were revealed.

Figure 1. Structure model of oxygen-evolving photosystem II from T. vulcanus

Figure 2. Arrangements of chlorophylls and other cofactors and their relative distances

Figure 3. Mn cluster and the electron density surrounding it

[ N. Kamiya and J.-R. Shen, Proceedings of National Academy of Science of the USA 100, 98-103 (2003), Fig. 1, 3, 4,
©2003 National Academy of Science ]

 

Source of the figure

Original paper/Journal article

Journal title

N. Kamiya, J. R. Shen Proc. Natl. Acad. Sci. U. S. A. 100, 98-103 (2003)

Figure No.

1,3,4

Technique

Source of the figure

No figure

Required time for experimental setup

hour(s)

Instruments

Instrument Purpose Performance
Protein Crystal Diffractometer To record diffraction data

References

Document name
N. Kamiya, J. R. Shen Proc. Natl. Acad. Sci. U. S. A. 100, 98-103 (2003)

Related experimental techniques

Questionnaire

The measurement was possible only in SPring-8. Impossible or very difficult in other facilities.
This solution is an application of a main instrument of the beamline.

Ease of measurement

Middle

Ease of analysis

Middle

How many shifts were needed for taking whole data in the figure?

More than ten shifts

Last modified 2022-05-06 15:34