SPring-8, the large synchrotron radiation facility

Inquiry number

SOL-0000001165

Beamline

BL41XU (Macromolecular Crystallography I)

Scientific keywords

A. Sample category	atom, molecule, radical, biology, medicine
B. Sample category (detail)	atom, biomolecule, crystal, protein, pharmaceuticals
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, chemical bonding, molecular structure, local structure, structure analysis, charge density

Industrial keywords

level 1---Application area	Pharmaceuticals
level 2---Target	catalysis, drug design, process analytical technology (PAT)
level 3---Target (detail)	protein, drug
level 4---Obtainable information	interatomic distance, local structure, electronic state, chemical state, absolute configuration
level 5---Technique	X-ray diffraction

Classification

A80.34 catalysis, A80.50 Pharmaceuticals, M10.10 single crystal diffraction, M10.80 stress strain

Body text

Ferredoxin is a small protein distributing widely in nature, from bacteria to higher plants and animals. It has one or more iron-sulfur cluster, iron atoms binding to thiol base of cysteines in shape of [2Fe-2S], [3Fe-4S] or [4Fe-4S]. The iron-sulfur cluster functions as a redox center for electron transfer, and has other various functions that catalytic site of enzyme, structure stabilizing factor of protein etc.

In this case, atomic resolution structure of [4Fe-4S] ferredoxin from B. thermoproteolyticus is analyzed at 0.92 Å resolution (Fig. 1).

This result revealed that the [4Fe-4S] cluster of this enzyme is distorted (Fig. 2).

Figure 1. Schematic model of [4Fe-4S] ferredoxin from B. thermoproteolyticus.

Figure 2. [4Fe-4S] cluster of electron density map (left) and ORTEP model(right)

[ K. Fukuyama, T. Okada, Y. Kakuta and Y. Yakahashi, Journal of Molecular Biology 315, 1155-1166 (2002), Fig. 1, 4, 7,
©2002 Elsevier, Inc. ]

Source of the figure

Original paper/Journal article

Journal title

K. Fukuyama, et al., J. Mol. Biol., 315, 1155-66 (2002)

Figure No.

1,4,7

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
K. Fukuyama, et al., J. Mol. Biol., 315, 1155-66 (2002)

Related experimental techniques

Questionnaire

This solution is an application of a main instrument of the beamline.

Ease of measurement

Middle

Ease of analysis

With a great skill

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

Two-three shifts