Unknown

Dataset Information

0

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


ABSTRACT: 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, P4, C2 and P2(1)2(1)2(1), which diffract to 1.8, 2.1 and 2.0 angstroms, respectively. Phases for one of these crystal forms (P4) 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 P4 crystal form.

SUBMITTER: Vogeley L 

PROVIDER: S-EPMC2222576 | biostudies-literature | 2006 Apr

REPOSITORIES: biostudies-literature

altmetric image

Publications

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

Vogeley Lutz L   Luecke Hartmut H  

Acta crystallographica. Section F, Structural biology and crystallization communications 20060325 Pt 4


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, P4, C2 and P2(1)2(1)2(1), which diffract to 1.8, 2.1 and 2.0 angstroms, respectively. Phases for one of these crystal forms (P4) were obtained by SIRAS phasing using an iodide quick-soak derivative and a partial model  ...[more]

Similar Datasets

| S-EPMC3515382 | biostudies-literature
| S-EPMC5791768 | biostudies-literature
| S-EPMC2041937 | biostudies-literature
| S-EPMC8660804 | biostudies-literature
| S-EPMC3267196 | biostudies-literature
| S-EPMC3003014 | biostudies-literature
| S-EPMC7842209 | biostudies-literature