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Small-angle X-ray scattering
Tsuruta, H. and Johnson, J. E.  International Tables for Crystallography (2012). Vol. F, ch. 19.3, pp. 563-574 [ doi:10.1107/97809553602060000869 ]
... crystal X-ray scattering, i.e. small-angle single-crystal diffraction (Tsuruta et al., 1998; Miller et al., 1999). The majority ... more robust if the low-resolution data are measured accurately (Tsuruta et al., 1998). Figure 19.3.2.2 | | Comparison of the absolute ... the bisubstrate analogue N-phosphoneacetyl-L-aspartate (E. R. Johnson, H. Tsuruta & H. K. Schachman, unpublished data). Other information ...

Time-resolved studies
Tsuruta, H. and Johnson, J. E.  International Tables for Crystallography (2012). Vol. F, Section 19.3.3.4.2, p. 572 [ doi:10.1107/97809553602060000869 ]
... studies of the allosteric transition of E. coli aspartate transcarbamoylase (Tsuruta et al., 1994), a structural intermediate during the enzyme reaction ... Top. Curr. Chem. 151, 2-30. Potschka, M., Koch, M. H. J., Adams, M. L. & Schuster, T. M. (1988). Time ... protein: kinetics and structure of intermediates. Biochemistry, 27, 8481-8491. Tsuruta, H., Vachette, P., Sano, T., Moody, M. F., Amemiya, ...
     [more results from section 19.3.3 in volume F]

Small-angle single-crystal X-ray diffraction studies
Tsuruta, H. and Johnson, J. E.  International Tables for Crystallography (2012). Vol. F, Section 19.3.2, pp. 563-564 [ doi:10.1107/97809553602060000869 ]
... crystal X-ray scattering, i.e. small-angle single-crystal diffraction (Tsuruta et al., 1998; Miller et al., 1999). The majority ... more robust if the low-resolution data are measured accurately (Tsuruta et al., 1998). Figure 19.3.2.2 | | Comparison of the absolute ... low resolution protein data. J. Appl. Cryst. 32, 1183-1185. Tsuruta, H., Reddy, V., Wikoff, W. & Johnson, J. (1998). ...

Introduction
Tsuruta, H. and Johnson, J. E.  International Tables for Crystallography (2012). Vol. F, Section 19.3.1, p. 563 [ doi:10.1107/97809553602060000869 ]
Introduction 19.3.1. Introduction Mechanistic biology is frequently confronted with an experimental paradox. High-resolution structures are required to develop a chemical description of macromolecular interactions, but the processes themselves are dynamic and not amenable to high-resolution methods. Chemists and molecular biologists have been successful in generating homogeneous components and entire ...

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