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MOLREP: an Automated Program for Molecular Replacement
MOLREP is an automated program for molecular replacement which utilizes effective new approaches in data processing and rotational and translational searching. These include an automatic choice of…
Molecular replacement with MOLREP.
MOLREP is an automated program for molecular replacement that utilizes a number of original approaches to rotational and translational search and data preparation that includes weighting of the X-ray data and search models, multi-copy search, fitting the model into electron density, structural superposition of two models and rigid-body refinement.
An approach to multi-copy search in molecular replacement.
The molecular-replacement method has been extended to a simultaneous search for multiple copies of the macromolecule in the unit cell using a special translation function and implemented in the program MOLREP and successfully tested using experimental data.
Crystal structure of neurotoxin Ts1 from Tityus serrulatus provides insights into the specificity and toxicity of scorpion toxins.
- I. Polikarpov, M. Júnior, S. Marangoni, M. Toyama, A. Teplyakov
- Chemistry, BiologyJournal of molecular biology
- 2 July 1999
Comparing Ts1 to weak beta-toxins from Centruroides sculpturatus Ewing reveals that a number of basic amino acid residues located on the face of the molecule opposite to the binding surface may account for the high toxicity of Ts1.
Evidence for a novel GTPase priming step in the SRP protein targeting pathway
It is proposed that the distinctive features of the SRP pathway GTPases evolved to ensure that SRP and the SR engage external ligands before interacting with each other.
Channeling of ammonia in glucosamine-6-phosphate synthase.
- A. Teplyakov, G. Obmolova, B. Badet, M. Badet-Denisot
- Biology, ChemistryJournal of molecular biology
- 9 November 2001
The crystal structure of the Escherichia coli enzyme reveals the domain organisation of the homodimeric molecule, and a mechanism of enzyme action and self-regulation is proposed that involves large domain movements triggered by substrate binding that lead to the formation of the channel.
The mechanism of sugar phosphate isomerization by glucosamine 6‐phosphate synthase
- A. Teplyakov, G. Obmolova, M. Badet-Denisot, B. Badet
- Chemistry, BiologyProtein science : a publication of the Protein…
- 31 December 2008
The information on ligand‐protein interactions observed in the crystal structures together with the isotope exchange and site‐directed mutagenesis data allow us to propose a mechanism of the isomerase activity of glucosamine‐6P synthase.
X-ray structure of yeast inorganic pyrophosphatase complexed with manganese and phosphate.
The three-dimensional structure of the manganese-phosphate complex of inorganic pyrophosphatase from Saccharomyces cerevisiae has been refined to an R factor of 19.0% at 2.4-A resolution and a hypothesis for the transition state of the catalytic reaction is put forward.
The ultimate wavelength for protein crystallography?
- I. Polikarpov, A. Teplyakov, G. Oliva
- PhysicsActa crystallographica. Section D, Biological…
- 1 November 1997
It is shown that there is no ultimate X-ray wavelength for protein crystallography and that the optimum wavelength depends to a large extent on the size of the protein crystal.
The structure of deoxy- and oxy-leghaemoglobin from lupin.
The only feature capable of accounting for the high on-rate of the reaction with oxygen are the mobilities of the proximal histidine and distal histidine residues in deoxy-leghaemoglobin and the oscillation of the imidazole between the two orientations.