000083589 001__ 83589
000083589 005__ 20180127195305.0
000083589 0247_ $$2doi$$a10.1002/(SICI)1097-0134(19980101)30:1<61::AID-PROT6>3.0.CO;2-N
000083589 037__ $$aARTICLE
000083589 245__ $$aExploring hydrophobic sites in proteins with xenon or krypton
000083589 269__ $$a1998
000083589 260__ $$c1998
000083589 336__ $$aJournal Articles
000083589 520__ $$aX-ray diffraction is used to study the binding of xenon and krypton to a variety of crystallised proteins: porcine pancreatic elastase; subtilisin Carlsberg from Bacillus licheniformis; cutinase from Fusarium solani; collagenase from Hypoderma lineatum; hen egg lysozyme, the lipoamide dehydrogenase domain from the outer membrane protein P64k from Neisseria meningitidis; urate-oxidase from Aspergillus flavus, mosquitocidal delta-endotoxin CytB from Bacillus thuringiensis and the ligand-binding domain of the human nuclear retinoid-X receptor RXR-alpha. Under gas pressures ranging from 8 to 20 bar, xenon is able to bind to discrete sites in hydrophobic cavities, ligand and substrate binding pockets, and into the pore of channel-like structures, These xenon complexes can be used to map hydrophobic sites in proteins, or as heavy-atom derivatives in the isomorphous replacement method of structure determination. (C) 1998 Wiley-Liss, Inc.
000083589 700__ $$aPrange, T.
000083589 700__ $$0240289$$aSchiltz, M.$$g158694
000083589 700__ $$aPernot, L.
000083589 700__ $$aColloc'h, N.
000083589 700__ $$aLonghi, S.
000083589 700__ $$aBourguet, W.
000083589 700__ $$aFourme, R.
000083589 773__ $$j30$$k1$$q61-73$$tProteins: Structure Function and Genetics
000083589 909C0 $$0252038$$pLCR
000083589 909CO $$ooai:infoscience.tind.io:83589$$particle$$pSB
000083589 937__ $$aLCR-ARTICLE-1998-002
000083589 973__ $$aOTHER$$rREVIEWED$$sPUBLISHED
000083589 980__ $$aARTICLE