Source:http://linkedlifedata.com/resource/pubmed/id/10329771
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
Pt 6
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pubmed:dateCreated |
1999-8-13
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pubmed:abstractText |
FixL is a transmitter protein in a two-component system which acts as an oxygen sensor when the symbiotic Rhizobia resides in root nodules of host plants. The oxygen-sensor domain of Rhizobium meliloti FixL (RmFixLH) was purified by His-tag affinity and isoelectronic focusing chromatographies, without the use of gel-filtration chromatography. Dynamic light-scattering measurements of RmFixLH thus obtained revealed it to be monodispersive and present as a homodimer in solution. A single crystal of RmFixLH in the met (Fe3+) form was grown in 100 mM acetic acid/NaOH buffer at pH 4.6 in the presence of 200 mM ammonium acetate, using 40%(w/v) PEG 4000 as a precipitant. A crystal of the ferrous CO form of RmFixLH was also prepared by reduction of the met crystal with Na2S2O4 in an atmosphere of CO. The crystals (0.2 x 0.05 x 0.01 mm) belong to the monoclinic system (C2) with unit-cell parameters a = 60.94, b = 37.44, c = 54.14 A, beta = 115.29 degrees and diffract X-rays to 1.7 A resolution at station BL44B2 of SPring-8, Japan. Bijvoet difference Patterson maps show a clear peak corresponding to the haem iron in RmFixLH.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0907-4449
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
55
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1215-8
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pubmed:dateRevised |
2007-7-24
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pubmed:meshHeading |
pubmed-meshheading:10329771-Bacterial Proteins,
pubmed-meshheading:10329771-Crystallography, X-Ray,
pubmed-meshheading:10329771-Hemeproteins,
pubmed-meshheading:10329771-Light,
pubmed-meshheading:10329771-Oxygen,
pubmed-meshheading:10329771-Protein Conformation,
pubmed-meshheading:10329771-Scattering, Radiation,
pubmed-meshheading:10329771-Sinorhizobium meliloti,
pubmed-meshheading:10329771-Spectrometry, Fluorescence
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pubmed:year |
1999
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pubmed:articleTitle |
Dynamic light-scattering and preliminary crystallographic studies of the sensor domain of the haem-based oxygen sensor FixL from Rhizobium meliloti.
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pubmed:affiliation |
The Institute of Physical and Chemical Research (RIKEN), RIKEN Harima Institute, 323-3 Mikazuki-cho, Mihara, Sayo, Hyogo 679-5143, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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