Use my Search Websuite to scan PubMed, PMCentral, Journal Hosts and Journal Archives, FullText. Kick-your-searchterm to multiple Engines kick-your-query now !>

A dictionary by aggregated review articles of nephrology, medicine and the life sciences Your one-stop-run pathway from word to the immediate pdf of peer-reviewed on-topic knowledge.

10.1107/S1744309105041199 http://scihub22266oqcxt.onion/10.1107/S1744309105041199 16511268!2150922!16511268     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=16511268&cmd=llinks): Failed to open stream: HTTP request failed! HTTP/1.1 429 Too Many Requests in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 215       Acta+Crystallogr+Sect+F+Struct+Biol+Cryst+Commun 2006 ; 62 (Pt 1): 77-9 Nephropedia Template TP {{tp|p=16511268|t=2006. Crystallization and preliminary X-ray diffraction analysis of a cold-adapted catalase from Vibrio salmonicida |pdf=|usr=}}{{16511268}} gab.com Text Crystallization and preliminary X-ray diffraction analysis of a cold-adapted catalase from Vibrio salmonicida JO: Acta Crystallogr Sect F Struct Biol Cryst Commun http://www.kidney.de/pget.php?&tw=1&pmid=16511268 #FOAvip Catalase (EC 1.11.1.6) catalyses the breakdown of hydrogen peroxide to water and molecular oxygen. Recombinant Vibrio salmonicida catalase (VSC) possesses typical cold-adapted features, with higher catalytic efficiency, lower thermal stability and a lower temperature optimum than its mesophilic counterpart from Proteus mirabilis. Crystals of VSC were produced by the hanging-drop vapour-diffusion method using ammonium sulfate as precipitant. The crystals belong to the monoclinic space group P2(1), with unit-cell parameters a = 98.15, b = 217.76, c = 99.28 A, beta = 110.48 degrees. Data were collected to 1.96 A and a molecular-replacement solution was found with eight molecules in the asymmetric unit. Twit Text FOAVip Crystallization and preliminary X-ray diffraction analysis of a cold-adapted catalase from Vibrio salmonicida ????Acta Crystallogr Sect F Struct Biol Cryst Commun http://www.kidney.de/pget.php?&tw=1&pmid=16511268 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=16511268 #FOAvip English Wikipedia <ref>{{Cite pmid|16511268}}</ref> Crystallization and preliminary X-ray diffraction analysis of a cold-adapted catalase from Vibrio salmonicida #MMPMID16511268 Riise EK; Lorentzen MS; Helland R; Willassen NP Acta Crystallogr Sect F Struct Biol Cryst Commun 2006[Jan]; 62 (Pt 1): 77-9 PMID16511268show ga Catalase (EC 1.11.1.6) catalyses the breakdown of hydrogen peroxide to water and molecular oxygen. Recombinant Vibrio salmonicida catalase (VSC) possesses typical cold-adapted features, with higher catalytic efficiency, lower thermal stability and a lower temperature optimum than its mesophilic counterpart from Proteus mirabilis. Crystals of VSC were produced by the hanging-drop vapour-diffusion method using ammonium sulfate as precipitant. The crystals belong to the monoclinic space group P2(1), with unit-cell parameters a = 98.15, b = 217.76, c = 99.28 A, beta = 110.48 degrees. Data were collected to 1.96 A and a molecular-replacement solution was found with eight molecules in the asymmetric unit. |*Cold Temperature[MESH] |Adaptation, Biological[MESH] |Aliivibrio salmonicida/*enzymology/physiology[MESH] |Amino Acid Sequence[MESH] |Catalase/*chemistry/physiology[MESH] |Catalysis[MESH] |Crystallization[MESH] |Crystallography, X-Ray[MESH] |Enzyme Stability[MESH] |Escherichia coli/genetics[MESH] |Models, Molecular[MESH] |Molecular Sequence Data[MESH] |Proteus mirabilis/enzymology[MESH] |Recombinant Proteins/chemistry[MESH]Crystallization and preliminary X-ray diffraction analysis of a cold-a(epmc).pdf DeepDyve Pubget Overpricing