5ynx: Difference between revisions

<table><tr><td colspan='2'>[[5ynx]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YNX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5YNX FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene>, <scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ynx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ynx OCA], [http://pdbe.org/5ynx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ynx RCSB], [http://www.ebi.ac.uk/pdbsum/5ynx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ynx ProSAT]</span></td></tr>

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Dermatophagoides farinae is one of the major house dust mite (HDM) species that cause allergic diseases. N-terminally His-tagged recombinant Der f 21 (rDer f 21), a group 21 allergen, with the signal peptide truncated was successfully overexpressed in an Escherichia coli expression system. The purified rDer f 21 protein was initially crystallized using the sitting-drop vapour-diffusion method. Well diffracting protein crystals were obtained after optimization of the crystallization conditions using the hanging-drop vapour-diffusion method with a reservoir solution consisting of 0.19 M Tris-HCl pH 8.0, 32% PEG 400 at 293 K. X-ray diffraction data were collected to 1.49 A resolution using an in-house X-ray source. The crystal belonged to the C-centered monoclinic space group C2, with unit-cell parameters a = 123.46, b = 27.71, c = 90.25 A, beta = 125.84 degrees . The calculated Matthews coefficient (VM) of 2.06 A(3) Da(-1) suggests that there are two molecules per asymmetric unit, with a solvent content of 40.3%. Despite sharing high sequence identity with Blo t 5 (45%) and Blo t 21 (41%), both of which were determined to be monomeric in solution, size-exclusion chromatography, static light scattering and self-rotation function analysis indicate that rDer f 21 is likely to be a dimeric protein.

 

Cloning, expression, purification, characterization, crystallization and X-ray crystallographic analysis of recombinant Der f 21 (rDer f 21) from Dermatophagoides farinae.,Pang SL, Ho KL, Waterman J, Teh AH, Chew FT, Ng CL Acta Crystallogr F Struct Biol Commun. 2015 Nov;71(Pt 11):1396-400. doi:, 10.1107/S2053230X1501818X. Epub 2015 Oct 23. PMID:26527267<ref>PMID:26527267</ref>

 

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<references/>

[[Category: Beis, K]]

[[Category: Chew, F T]]

[[Category: Ho, K L]]

[[Category: Mathavan, I]]

[[Category: Ng, C L]]

[[Category: Pang, S L]]

[[Category: Rambo, R]]

[[Category: Say, Y H]]

[[Category: Teh, A H]]

[[Category: Waterman, J]]

[[Category: Allergen]]