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S D Trakhanov

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Articles 7
Citations 82
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1.
Segelke B, Forstner M, Knapp M, Trakhanov S, Parkin S, Newhouse Y, et al.
Protein Sci . 2000 Jun; 9(5):886-97. PMID: 10850798
An amino-terminal fragment of human apolipoprotein E3 (residues 1-165) has been expressed and crystallized in three different crystal forms under similar crystallization conditions. One crystal form has nearly identical cell...
2.
Dong L, Parkin S, Trakhanov S, Rupp B, Simmons T, Arnold K, et al.
Nat Struct Biol . 1996 Aug; 3(8):718-22. PMID: 8756331
The defective binding of apolipoprotein (apo) E2 to lipoprotein receptors, an underlying cause of type III hyperlipoproteinemia, results from replacement of Arg 158 with Cys, disrupting the naturally occurring salt...
3.
Mikhailov A, Nikitenko A, Chetverina E, Trakhanov S, Vainshten B
Bioorg Khim . 1991 Mar; 17(3):372-8. PMID: 2064629
The structure of the alpha-carbon chain was solved by molecular replacement method at 2.7 A resolution. Neurotoxin I (NTX-I) is one of the main protein components purified from the venom...
4.
Mikhailov A, Nickitenko A, Trakhanov S, Vainshtein B, Chetverina E
FEBS Lett . 1990 Aug; 269(1):255-7. PMID: 2387409
Crystals of the neurotoxin-I (NTX-I) from the venom of the middle Asian cobra Naja naja oxiana have been grown by vapour diffusion and dialysis methods. The crystals belong to space...
5.
Trakhanov S, Chirgadze NYu , Yusifov E
J Mol Biol . 1989 Jun; 207(4):847-9. PMID: 2668541
Histidine-binding protein, purified from periplasmic space of Escherichia coli K12, has been crystallized in a form suitable for X-ray analysis. Crystals of average size 0.3 mm x 0.15 mm x...
6.
Trakhanov S
Bioorg Khim . 1989 Jun; 15(6):725-30. PMID: 2675849
Several variants of microdialysis cells have been developed for growing protein crystals suitable for X-ray analysis. The cells have simple construction and are made of easily available materials. Using these...
7.
Sack J, Trakhanov S, Tsigannik I, Quiocho F
J Mol Biol . 1989 Mar; 206(1):193-207. PMID: 2649683
The three-dimensional X-ray structure of the leucine-binding protein (36,900 Mr and 346 residues), an active transport component of Escherichia coli, has been determined by the method of molecular replacement, using...