International
Tables for
Crystallography
Volume F
Crystallography of biological macromolecules
Edited by E. Arnold, D. M. Himmel and M. G. Rossmann

International Tables for Crystallography (2012). Vol. F, ch. 8.1, p. 200   | 1 | 2 |

Section 8.1.9. Concluding remarks

J. R. Helliwella*

aDepartment of Chemistry, University of Manchester, M13 9PL, England
Correspondence e-mail: john.helliwell@manchester.ac.uk

8.1.9. Concluding remarks

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SR and crystallography are now intricately intertwined in their scientific futures and in facilities provision (see e.g. Helliwell, 1998[link]; Dauter, 2006[link]; Fig. 8.1.9.1[link]). Jiang & Sweet (2004)[link] have given a systematic analysis of the impact of SR on macromolecular crystallography capabilities.

[Figure 8.1.9.1]

Figure 8.1.9.1 | top | pdf |

Synchrotron structures deposited in the PDB versus all PDB deposited structures (from http://biosync.rcsb.org/BiosyncStat.html ) as of December 2009, i.e. a majority of all determined macromolecular crystal structures are now synchrotron-radiation derived.

The new XFELs have produced very novel possibilities for 3D structure determination not only of non-crystallizable proteins but also whole cells (Neutze et al., 2000[link]; Miao et al., 2001[link]; Sayre, 2008[link]; Shapiro, 2008[link]). Whilst these approaches have attracted controversy, they represent a bold new push of X-ray diffraction methods towards widening capabilities in important frontiers in structural biology and structural cellular biology.

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