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Figure 5
Comparison of in situ and frozen data collection from crystals of a protein–DNA complex. View of a crystal in a drop within a crystallization plate (a) and the diffraction obtained from this sample (b). Spots were observed to 10 Å resolution. A crystal grown in identical conditions was mounted in a fibre loop and cryocooled to 100 K (c). The resulting diffraction extended no further than 35 Å resolution (d) from the cryocooled crystal despite it being a larger size. In situ data collection allows a much more accurate assessment of crystallization conditions during the process of crystallization optimization.

Journal logoSTRUCTURAL
ISSN: 2059-7983
Volume 68| Part 5| May 2012| Pages 592-600
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