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| | <StructureSection load='6irk' size='340' side='right'caption='[[6irk]], [[Resolution|resolution]] 1.75Å' scene=''> | | <StructureSection load='6irk' size='340' side='right'caption='[[6irk]], [[Resolution|resolution]] 1.75Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6irk]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Streptomyces_rubiginosus Streptomyces rubiginosus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6IRK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6IRK FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6irk]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_rubiginosus Streptomyces rubiginosus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6IRK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6IRK FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.75Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Xylose_isomerase Xylose isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.5 5.3.1.5] </span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=6irk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6irk OCA], [http://pdbe.org/6irk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6irk RCSB], [http://www.ebi.ac.uk/pdbsum/6irk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6irk ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6irk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6irk OCA], [https://pdbe.org/6irk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6irk RCSB], [https://www.ebi.ac.uk/pdbsum/6irk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6irk ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/XYLA_STRRU XYLA_STRRU]] Involved in D-xylose catabolism. | + | [https://www.uniprot.org/uniprot/XYLA_STRRU XYLA_STRRU] Involved in D-xylose catabolism. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 6irk" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 6irk" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[D-xylose isomerase 3D structures|D-xylose isomerase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| | [[Category: Streptomyces rubiginosus]] | | [[Category: Streptomyces rubiginosus]] |
| - | [[Category: Xylose isomerase]]
| + | [[Category: Nam KH]] |
| - | [[Category: Nam, K H]] | + | |
| - | [[Category: Isomerase]]
| + | |
| - | [[Category: Sfx]]
| + | |
| Structural highlights
Function
XYLA_STRRU Involved in D-xylose catabolism.
Publication Abstract from PubMed
Fixed-target serial femtosecond crystallography (FT-SFX) was an important advance in crystallography by dramatically reducing sample consumption, while maintaining the benefits of SFX for obtaining crystal structures at room temperature without radiation damage. Despite a number of advantages, preparation of a sample holder for the sample delivery in FT-SFX with the use of many crystals in a single mount at ambient temperature is challenging as it can be complicated and costly, and thus, development of an efficient sample holder is essential. In this study, we introduced a nylon mesh-based sample holder enclosed by a polyimide film. This sample holder can be rapidly manufactured using a commercially available nylon mesh with pores of a desired size at a low cost without challenging technology. Furthermore, this simple device is highly efficient in data acquisition. We performed FT-SFX using a nylon mesh-based sample holder and collected over 130,000 images on a single sample holder using a 30 Hz X-ray pulse for 1.2 h. We determined the crystal structures of lysozyme and glucose isomerase using the nylon mesh at 1.65 and 1.75 A, respectively. The nylon mesh exposed to X-rays produced very low levels of background scattering at 3.75 and 4.30 A, which are negligible for data analysis. Our method provides a simple and rapid but highly efficient way to deliver samples for FT-SFX.
Nylon mesh-based sample holder for fixed-target serial femtosecond crystallography.,Lee D, Baek S, Park J, Lee K, Kim J, Lee SJ, Chung WK, Lee JL, Cho Y, Nam KH Sci Rep. 2019 May 6;9(1):6971. doi: 10.1038/s41598-019-43485-z. PMID:31061502[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Lee D, Baek S, Park J, Lee K, Kim J, Lee SJ, Chung WK, Lee JL, Cho Y, Nam KH. Nylon mesh-based sample holder for fixed-target serial femtosecond crystallography. Sci Rep. 2019 May 6;9(1):6971. doi: 10.1038/s41598-019-43485-z. PMID:31061502 doi:http://dx.doi.org/10.1038/s41598-019-43485-z
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