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10.1111/j.1742-4658.2007.06178.x http://scihub22266oqcxt.onion/10.1111/j.1742-4658.2007.06178.x C4465431!4465431 !18034855     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=18034855 &cmd=llinks): Failed to open stream: HTTP request failed! 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Protein crystallography for non-crystallographers, or how to get the best (but not more) from published macromolecular structures |pdf=|usr=}}{{18034855 }} gab.com Text Protein crystallography for non-crystallographers, or how to get the best (but not more) from published macromolecular structures JO: FEBS J http://www.kidney.de/pget.php?&tw=1&pmid=18034855 #FOAvip The number of macromolecular structures deposited in the Protein Data Bank now exceeds 45,000, with the vast majority determined using crystallographic methods. Thousands of studies describing such structures have been published in the scientific literature, and 14 Nobel prizes in chemistry or medicine have been awarded to protein crystallographers. As important as these structures are for understanding the processes that take place in living organisms and also for practical applications such as drug design, many non-crystallographers still have problems with critical evaluation of the structural literature data. This review attempts to provide a brief outline of technical aspects of crystallography and to explain the meaning of some parameters that should be evaluated by users of macromolecular structures in order to interpret, but not over-interpret, the information present in the coordinate files and in their description. A discussion of the extent of the information that can be gleaned from the coordinates of structures solved at different resolution, as well as problems and pitfalls encountered in structure determination and interpretation are also covered. Twit Text FOAVip Protein crystallography for non-crystallographers, or how to get the best (but not more) from published macromolecular structures ????FEBS J http://www.kidney.de/pget.php?&tw=1&pmid=18034855 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=18034855 #FOAvip English Wikipedia <ref>{{Cite pmid|18034855 }}</ref> Protein crystallography for non-crystallographers, or how to get the best (but not more) from published macromolecular structures #MMPMID18034855 Wlodawer A ; Minor W ; Dauter Z ; Jaskolski M FEBS J 2008[Jan]; 275 (1 ): 1-21 PMID18034855 show ga The number of macromolecular structures deposited in the Protein Data Bank now exceeds 45,000, with the vast majority determined using crystallographic methods. Thousands of studies describing such structures have been published in the scientific literature, and 14 Nobel prizes in chemistry or medicine have been awarded to protein crystallographers. As important as these structures are for understanding the processes that take place in living organisms and also for practical applications such as drug design, many non-crystallographers still have problems with critical evaluation of the structural literature data. This review attempts to provide a brief outline of technical aspects of crystallography and to explain the meaning of some parameters that should be evaluated by users of macromolecular structures in order to interpret, but not over-interpret, the information present in the coordinate files and in their description. A discussion of the extent of the information that can be gleaned from the coordinates of structures solved at different resolution, as well as problems and pitfalls encountered in structure determination and interpretation are also covered. |*Crystallography, X-Ray/standards [MESH] |*Protein Conformation [MESH] |Animals [MESH] |Databases, Protein [MESH] |Humans [MESH] |Models, Molecular [MESH] |Molecular Structure [MESH] |Proteins/chemistry [MESH]Protein crystallography for non-crystallographers, or how to get the b(epmc).pdf DeepDyve Pubget Overpricing