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obtained after ir<strong>radiation</strong> of the samples for up to 3 h at one wavelength<br />

in the UV range ( 220±230 nm). The results from the present<br />

study seem somewhat incompatible with those observations, in that<br />

ir<strong>radiation</strong> over the entire range from 160 to 300 nm at much higher<br />

intensities produced no such detectable changes. The samples in the<br />

previous studies were not characterized in terms of their chemical<br />

integrity following the procedures. The present studies, however,<br />

have included careful characterizations of the protein by both gel<br />

electrophoresis and mass spectrometry to demonstrate the lack of<br />

chemical modi®cation to the protein as a result of any of the handling<br />

or ir<strong>radiation</strong> procedures.<br />

In summary, ir<strong>radiation</strong> of myoglobin at VUV wavelengths in the<br />

SRCD appears to have resulted in no damage, crosslinking or cleavage<br />

of the protein, despite the high intensity of the beam. Thus, it<br />

should be possible to make SRCD measurements over a considerable<br />

period of time without concern of altering the chemistry or structure<br />

of the sample.<br />

We thank Neil Freeman of GlaxoSmithKline and Dr Peter Bayley<br />

of NIMR for helpful discussions, and the staff and scientists of station<br />

research papers<br />

3.1 at Daresbury and station UV1 at ASTRID for use of the facilities.<br />

We acknowledge the BBSRC for provision of beam time at the SRS.<br />

This work was supported by a grant from the BBSRC to BAW. AJWO<br />

was supported by a BBSRC studentship and MH was supported by a<br />

project grant from the Wellcome Trust to BAW.<br />

References<br />

Clarke, D. T., Bowler, M. A., Fell, B. D., Flaherty, J. V., Grant, A. F., Jones,<br />

G. R., Martin-Fernandez, M. L., Shaw, D. A., Todd, B., Wallace, B. A. &<br />

Towns-Andrews, E. (2000). <strong>Synchrotron</strong> Rad. News, 13, 21±27.<br />

Johnson, W. C. Jr (1978). Ann. Rev. Phys. Chem. 29, 93±114.<br />

Snyder, P. A. & Rowe, E. M. (1980). Nucl. Instrum. Methods, 172, 345±349.<br />

Sutherland, J. C., Desmond, E. J. & Takacs, P. Z. (1980). Nucl. Instrum.<br />

Methods, 172, 195±199.<br />

Takeda, K. & Moriyama, Y. (1991). J. Am. Chem. Soc. 113, 6700±6701.<br />

Wallace, B. A. (2000a). J. <strong>Synchrotron</strong> Rad. 7, 289±295.<br />

Wallace, B. A. (2000b). Nature Struct. Biol. 7, 708±709.<br />

Wallace, B. A., Janes, R. W. & Orry, A. (2001). Biophys. J. 80, 28a.<br />

Wilson, W. D. & Foster, J. F. (1970). Biochem. Biophys. Res. Commun. 38, 552±<br />

558.<br />

J. <strong>Synchrotron</strong> Rad. (2001). 8, 1027±1029 Received 5 February 2001 Accepted 12 March 2001 1029<br />

<strong>electronic</strong> <strong>reprint</strong>

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