Crystallization, X‐ray diffraction analysis and SIRAS/molecular‐replacenent phasing of three crystal forms of  Anabaena  sensory rhodopsin transducer | Zendy

Vogeley Lutz | Zendy; Luecke Hartmut | Zendy

Open Access

Crystallization, X‐ray diffraction analysis and SIRAS/molecular‐replacenent phasing of three crystal forms of Anabaena sensory rhodopsin transducer

Author(s) -

Vogeley Lutz,

Luecke Hartmut

Publication year - 2006

Publication title -

acta crystallographica section f

Language(s) - English

Resource type - Journals

ISSN - 1744-3091

DOI - 10.1107/s1744309106008359

Subject(s) - rhodopsin , crystal (programming language) , crystallization , anabaena , crystallography , diffraction , sensory system , iodide , molecular replacement , materials science , crystal structure , chemistry , biology , physics , cyanobacteria , optics , biochemistry , inorganic chemistry , organic chemistry , computer science , retinal , programming language , neuroscience , bacteria , genetics

Anabaena sensory rhodopsin transducer (ASRT) is a 14.7 kDa soluble signaling protein associated with the membrane‐embedded light receptor Anabaena sensory rhodopsin (ASR) from Anabaena sp., a freshwater cyanobacterium. Crystals of ASRT were obtained in three different space groups, P 4, C 2 and P 2 1 2 1 2 1 , which diffract to 1.8, 2.1 and 2.0 Å, respectively. Phases for one of these crystal forms ( P 4) were obtained by SIRAS phasing using an iodide quick‐soak derivative and a partial model was built. Phases for the remaining crystal forms were obtained by molecular replacement using the partial model from the P 4 crystal form.

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