17617922

Source:http://linkedlifedata.com/resource/pubmed/id/17617922

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Predicate	Object
rdf:type	pubmed:Citation
lifeskim:mentions	umls-concept:C0010423, umls-concept:C0337611, umls-concept:C0558269, umls-concept:C0597094, umls-concept:C1269765
pubmed:dateCreated	2007-8-8
pubmed:databankReference	http://linkedlifedata.com/resource/pubmed/xref/PDB/1VK1
pubmed:abstractText	The major bottleneck for determination of 3 D structures of proteins using X-rays is the production of diffraction quality crystals. Often proteins are subjected to chemical modification to improve the chances of crystallization
pubmed:commentsCorrections	http://linkedlifedata.com/resource/pubmed/commentcorrection/17617922-10489469, http://linkedlifedata.com/resource/pubmed/commentcorrection/17617922-10535950, http://linkedlifedata.com/resource/pubmed/commentcorrection/17617922-11463918, http://linkedlifedata.com/resource/pubmed/commentcorrection/17617922-12137514, http://linkedlifedata.com/resource/pubmed/commentcorrection/17617922-12718922, http://linkedlifedata.com/resource/pubmed/commentcorrection/17617922-15062076, http://linkedlifedata.com/resource/pubmed/commentcorrection/17617922-15107015, http://linkedlifedata.com/resource/pubmed/commentcorrection/17617922-15317594, http://linkedlifedata.com/resource/pubmed/commentcorrection/17617922-15689503, http://linkedlifedata.com/resource/pubmed/commentcorrection/17617922-17098187, http://linkedlifedata.com/resource/pubmed/commentcorrection/17617922-5690712, http://linkedlifedata.com/resource/pubmed/commentcorrection/17617922-7061454, http://linkedlifedata.com/resource/pubmed/commentcorrection/17617922-7287304, http://linkedlifedata.com/resource/pubmed/commentcorrection/17617922-7674305, http://linkedlifedata.com/resource/pubmed/commentcorrection/17617922-8060493, http://linkedlifedata.com/resource/pubmed/commentcorrection/17617922-8373783, http://linkedlifedata.com/resource/pubmed/commentcorrection/17617922-9048376, http://linkedlifedata.com/resource/pubmed/commentcorrection/17617922-9066260, http://linkedlifedata.com/resource/pubmed/commentcorrection/17617922-9641677, http://linkedlifedata.com/resource/pubmed/commentcorrection/17617922-9641985
pubmed:language	eng
pubmed:journal	http://linkedlifedata.com/resource/pubmed/journal/101088689
pubmed:citationSubset	IM
pubmed:chemical	http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Deoxyribonucleases, http://linkedlifedata.com/resource/pubmed/chemical/Endodeoxyribonucleases, http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Exodeoxyribonucleases, http://linkedlifedata.com/resource/pubmed/chemical/Lysine, http://linkedlifedata.com/resource/pubmed/chemical/dnaG protein, E coli
pubmed:status	MEDLINE
pubmed:issn	1472-6807
pubmed:author	pubmed-author:ChangJessieJ, pubmed-author:ChengChongyunC, pubmed-author:LiuZhi-JieZJ, pubmed-author:NgJosephJ, pubmed-author:PerrettSarahS, pubmed-author:RaoZiheZ, pubmed-author:RoseJohnJ, pubmed-author:ShawNeilN, pubmed-author:TempelWolframW, pubmed-author:WangBi-ChengBC, pubmed-author:WangXin-YuXY
pubmed:issnType	Electronic
pubmed:volume	7
pubmed:owner	NLM
pubmed:authorsComplete	Y
pubmed:pagination	46
pubmed:dateRevised	2009-11-18
pubmed:meshHeading	pubmed-meshheading:17617922-Bacterial Proteins, pubmed-meshheading:17617922-Crystallography, X-Ray, pubmed-meshheading:17617922-Deoxyribonucleases, pubmed-meshheading:17617922-Endodeoxyribonucleases, pubmed-meshheading:17617922-Escherichia coli Proteins, pubmed-meshheading:17617922-Exodeoxyribonucleases, pubmed-meshheading:17617922-Lysine, pubmed-meshheading:17617922-Methylation, pubmed-meshheading:17617922-Models, Molecular, pubmed-meshheading:17617922-Protein Structure, Secondary, pubmed-meshheading:17617922-Protein Structure, Tertiary, pubmed-meshheading:17617922-Pyrococcus furiosus, pubmed-meshheading:17617922-Thermodynamics
pubmed:year	2007
pubmed:articleTitle	(NZ)CH...O contacts assist crystallization of a ParB-like nuclease.
pubmed:affiliation	National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, China. neilshaw@moon.ibp.ac.cn <neilshaw@moon.ibp.ac.cn>
pubmed:publicationType	Journal Article, Research Support, Non-U.S. Gov't