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The final structure of NerA in its apo form was used as the molecular replacement template for the lower-resolution (2.45 and 2.29 Å) complex structures.
The loops connecting β strands 5 and 6 with their subsequent α-helices are rather shorter in NerA than in the molecular replacement template, PETNR (and other OYE-like proteins).
Using the known HsAPC-1 RD structure as a molecular replacement template [16] the structure of the HsAPC-1 RD was solved in two different space groups: to 2.1 Å resolution in space-group P2 from the square plate-like crystals, and to 2.6 Å in the space-group P212121 from the tetrahedral bi-pyramidal type crystals.
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The crystal structure of the equivalent fragment of the orthologue from wheat was used as a template for molecular replacement (PDB accession code 2IDV), with which the pea protein shares 71% amino acid sequence identity over this region (60% identity overall).
EstA was overexpressed and its crystal structure was solved by molecular replacement using a lipase-acetylcholinesterase chimera template.
After density modification with Parrot (Zhang et al., 1997) the protein backbone was rebuild into the density-modified map and a run of molecular replacement was started with the new template.
In preparation for a structure-function analysis of pea eIF4E in relation to PSbMV susceptibility we determined the crystal structure of pea eIF4EΔN51 by molecular replacement, using the wheat orthologue as a template [30].
The latter was in fact used as a template to build the model for the molecular replacement.
Both WDR5 co-crystal structures were determined by molecular replacement using the PDB code 2O9K model as the search template.
The structure was determined by molecular replacement using the published structure of 5-HTBP as the template (PDB: 2YMD).
Initial phasing was performed by molecular replacement using the structure of the human Fab PDB entry 1AQK as template and using the software Phaser [21].
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