In:
Acta Crystallographica Section D Biological Crystallography, International Union of Crystallography (IUCr), Vol. 55, No. 6 ( 1999-06-01), p. 1215-1218
Abstract:
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 (Fe 3+ ) form was grown in 100 m M acetic acid/NaOH buffer at pH 4.6 in the presence of 200 m M 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 Na 2 S 2 O 4 in an atmosphere of CO. The crystals (0.2 × 0.05 × 0.01 mm) belong to the monoclinic system ( C 2) with unit-cell parameters a = 60.94, b = 37.44, c = 54.14 Å, β = 115.29° and diffract X-rays to 1.7 Å resolution at station BL44B2 of SPring-8, Japan. Bijvoet difference Patterson maps show a clear peak corresponding to the haem iron in RmFixLH.
Type of Medium:
Online Resource
ISSN:
0907-4449
DOI:
10.1107/S0907444999004047
Language:
Unknown
Publisher:
International Union of Crystallography (IUCr)
Publication Date:
1999
detail.hit.zdb_id:
2968623-4
SSG:
12
SSG:
13
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