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| 024 | 7 | _ | |a 10.1107/S2053230X15011383 |2 doi |
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| 082 | _ | _ | |a 530 |
| 100 | 1 | _ | |a Ohlin, Mats |0 P:(DE-HGF)0 |b 0 |
| 245 | _ | _ | |a Crystallization, neutron data collection, initial structure refinement and analysis of a xyloglucan heptamer bound to an engineered carbohydrate-binding module from xylanase |
| 260 | _ | _ | |a Oxford [u.a.] |c 2015 |b Blackwell |
| 336 | 7 | _ | |a Journal Article |b journal |m journal |0 PUB:(DE-HGF)16 |s 1449471784_18275 |2 PUB:(DE-HGF) |
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| 336 | 7 | _ | |a ARTICLE |2 BibTeX |
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| 336 | 7 | _ | |a article |2 DRIVER |
| 520 | _ | _ | |a Carbohydrate-binding modules (CBMs) are discrete parts of carbohydrate-hydrolyzing enzymes that bind specific types of carbohydrates. Ultra high-resolution X-ray crystallographic studies of CBMs have helped to decipher the basis for specificity in carbohydrate-protein interactions. However, additional studies are needed to better understand which structural determinants confer which carbohydrate-binding properties. To address these issues, neutron crystallographic studies were initiated on one experimentally engineered CBM derived from a xylanase, X-2 L110F, a protein that is able to bind several different plant carbohydrates such as xylan, [beta]-glucan and xyloglucan. This protein evolved from a CBM present in xylanase Xyn10A of Rhodothermus marinus. The protein was complexed with a branched xyloglucan heptasaccharide. Large single crystals of hydrogenous protein (~1.6 mm3) were grown at room temperature and subjected to H/D exchange. Both neutron and X-ray diffraction data sets were collected to 1.6 Å resolution. Joint neutron and X-ray refinement using phenix.refine showed significant density for residues involved in carbohydrate binding and revealed the details of a hydrogen-bonded water network around the binding site. This is the first report of a neutron structure of a CBM and will add to the understanding of protein-carbohydrate binding interactions. |
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| 693 | _ | _ | |a Forschungs-Neutronenquelle Heinz Maier-Leibnitz |e BIODIFF: Diffractometer for large unit cells |f NL1 |1 EXP:(DE-MLZ)FRMII-20140101 |0 EXP:(DE-MLZ)BIODIFF-20140101 |5 EXP:(DE-MLZ)BIODIFF-20140101 |6 EXP:(DE-MLZ)NL1-20140101 |x 0 |
| 700 | 1 | _ | |a von Schantz, Laura |0 P:(DE-HGF)0 |b 1 |
| 700 | 1 | _ | |a Schrader, Tobias E. |0 P:(DE-Juel1)138266 |b 2 |u fzj |
| 700 | 1 | _ | |a Ostermann, Andreas |0 P:(DE-HGF)0 |b 3 |
| 700 | 1 | _ | |a Logan, Derek T. |0 P:(DE-HGF)0 |b 4 |
| 700 | 1 | _ | |a Fisher, S. Zoë |0 P:(DE-HGF)0 |b 5 |e Corresponding author |
| 773 | _ | _ | |a 10.1107/S2053230X15011383 |g Vol. 71, no. 8, p. 1072 - 1077 |0 PERI:(DE-600)2175956-X |n 8 |p 1072 - 1077 |t Acta crystallographica / F |v 71 |y 2015 |x 2053-230X |
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| 914 | 1 | _ | |y 2015 |
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