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100 | 1 | _ | |a Kaljunen, Heidi |0 P:(DE-H253)PIP1017942 |b 0 |e Corresponding Author |
245 | _ | _ | |a Cloning, Overexpression, Purification and Preliminary X-Ray Analysis of the Protein Kinase Domain of Enhanced Disease Resistance 1 (EDR1) from Arabidopsis Thaliana |
260 | _ | _ | |a Oxford [u.a.] |c 2014 |b Blackwell |
336 | 7 | _ | |a Journal Article |0 0 |2 EndNote |
336 | 7 | _ | |a article |2 DRIVER |
336 | 7 | _ | |a Journal Article |b journal |m journal |0 PUB:(DE-HGF)16 |s 1462366439_5565 |2 PUB:(DE-HGF) |
336 | 7 | _ | |a ARTICLE |2 BibTeX |
500 | _ | _ | |3 POF3_Assignment on 2016-02-15 |
500 | _ | _ | |3 POF3_Prefill: G:(DE-HGF)POF3-6215 |
500 | _ | _ | |a (c) International Union of Crystallography. Post referee full text in progress. |
520 | _ | _ | |a Enhanced disease resistance 1 is a member of the Raf-like mitogen-activated protein kinase kinase kinase (MAPKKK) family that negatively regulates disease resistance, ethylene-induced senescence and programmed cell death in response to both abiotic and biotic stresses. A catalytically inactive form of the EDR1 kinase domain was successfully cloned, expressed, purified and crystallized. Crystallization was conducted in the presence of the ATP analogue AMP-PNP. The crystals belonged to space group $P3_{2}21$ and contained two molecules in the asymmetric unit. The crystals diffracted X-rays to 2.55 Å resolution. |
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700 | 1 | _ | |a Mueller-Dieckmann, Jochen |0 P:(DE-HGF)0 |b 2 |
773 | _ | _ | |a 10.1107/S2053230X14011844 |0 PERI:(DE-600)2175956-X |n 7 |p 959-962 |t Acta crystallographica / F |v 70 |y 2014 |x 1744-3091 |
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