Open AccessCrystallization, preliminary X‐ray diffraction and structure solution of MosA, a dihydrodipicolinate synthase from Sinorhizobium meliloti L5‐30
Author(s) -
Leduc Yvonne A.,
Phenix Christopher P.,
Puttick Jennifer,
Nienaber Kurt,
Palmer David R. J.,
Delbaere Louis T. J.
Publication year - 2006
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309105040893
Subject(s) - sinorhizobium meliloti , orthorhombic crystal system , crystallography , crystallization , molecular replacement , atp synthase , epimer , x ray crystallography , biology , diffraction , chemistry , crystal structure , enzyme , stereochemistry , physics , biochemistry , bacteria , genetics , optics , symbiosis , organic chemistry
The structure of MosA, a dihydrodipicolinate synthase and reported methyltransferase from Sinorhizobium meliloti , has been solved using molecular replacement with Escherichia coli dihydrodipicolinate synthase as the model. A crystal grown in the presence of pyruvate diffracted X‐rays to 2.3 Å resolution using synchrotron radiation and belonged to the orthorhombic space group C 222 1 , with unit‐cell parameters a = 69.14, b = 138.87, c = 124.13 Å.