期刊
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY
卷 67, 期 -, 页码 376-385出版社
INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S0907444911007232
关键词
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资金
- Biotechnology and Biological Sciences Research Council (BBSRC) UK [721/B19544]
- BBSRC [BB/F020805/1, BB/F020228/1] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BB/F020805/1, BB/F020228/1] Funding Source: researchfish
This paper presents a discussion of existing methods for the analysis of macromolecular interactions and complexes in crystal packing. Typical situations and conditions where wrong answers may be obtained in the course of ordinary procedures are presented and discussed. The more general question of what the relationship is between natural (in-solvent) and crystallized assemblies is discussed and researched. A computational analysis suggests that weak interactions with K-d >= 100 mu M have a considerable chance of being lost during the course of crystallization. In such instances, crystal packing misrepresents macromolecular complexes and interactions. For as many as 20% of protein dimers in the PDB the likelihood of misrepresentation is estimated to be higher than 50%. Given that weak macromolecular interactions play an important role in many biochemical processes, these results suggest that a complementary noncrystallographic study should be always conducted when inferring structural aspects of weakly bound complexes.
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