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![[Figure 3]](ml2017fig3mag.jpg)
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Figure 3
The correct choice of protein crystal sample size is important for freezing. Diffraction pattern (a) involved too big a crystal (0.5–0.8 mm in size, minimum to maximum) and yielded high mosaicity and split spots. In (b), sharp single spots (not split) from a crystal of size 0.2 mm are shown and from which a full data set could be recorded and processed to 1.2 Å. Sample: disaccharide-bound concanavalin A (see Sanders et al., 2001  ). Methods to reach atomic resolution but at room temperature, which is, after all, closer to physiological temperature, seek to improve the reflection peak-to-background ratio by combining the synchrotron radiation beam near parallel collination with low-mosaicity crystals (Snell et al., 1999). Hence, the link between crystal growth, data collection and structural detail is made (Boggon et al., 2000). One can readily see how high-brilliance synchrotron radiation X-ray sources and their gradual evolution over these last 20 years (Ealick & Helliwell, 1999, and articles therein) has had such a profound effect on the data-collection capability in protein crystallography structural studies. |
![[Figure 3]](ml2017fig3.jpg)
 | JOURNAL OF SYNCHROTRON RADIATION |
ISSN: 1600-5775
