An approach to multi-copy search in molecular replacement.

By A. Vagin, A. Teplyakov. Acta Crystallographica Section D: Biological Crystallography, 2000

689 citations recorded by the source corpus.

View Paper: https://www.semanticscholar.org/paper/2d44ba45a11d5ff46b68c5abfcb27538cd9aee85

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Citations in the corpus

Anti‐Inflammatory Property of n‐Hexadecanoic Acid: Structural Evidence and Kinetic Assessment (2012, methodology): “Molecular replacement method (MOLREP) (28) was used to solve the crystal structure.”
Crystal structure of chondroitin polymerase from Escherichia coli K4. (2009, methodology): “The crystal structure of the UDP-GlcUA/UDP complex was determined by molecular replacement using the partially refined dimmer model as a search model with the Molrep program [12].”
Molecular replacement with MOLREP. (2010, methodology): “The MR method has been extended to a simultaneous search for multiple copies of the macromolecule in the unit cell (Vagin & Teplyakov, 2000).”
Improved Technologies Now Routinely Provide Protein NMR Structures Useful for Molecular Replacement (2011, methodology): “…improved the effectiveness of the MR approach, such as COMO (Jogl et al., 2001), XPLOR/CNS (Brunger et al., 1998), AMoRe (Navaza, 2001), MOLREP (Vagin and Teplyakov, 2000), EPMR (Kissinger et al., 1999), Queen of Spades (Glykos and Kokkinidis, 2000), SoMoRe (Jamrog et al., 2003), MrBUMP…”
Structure of a flavivirus envelope glycoprotein in its low‐pH‐induced membrane fusion conformation (2004, methodology): “…by molecular replacement using the available coordinates of the neutral pH, dimeric form of TBEV sE (Rey et al, 1995) and data from crystal forms O2 and T, using a combination of the ‘dyad search’ procedure implemented in Molrep (Vagin and Teplyakov, 2000) and the AMoRe package (Navaza, 1994).”
Computational design of a self-assembling symmetrical β-propeller protein (2014, methodology): “The computational models were used for molecular replacement using MOLREP (41), followed by refinement with Refmac5 (42) and PHENIX (43).”
Structural Dynamics of the Cereblon Ligand Binding Domain (2015, methodology): “The structures of the washed orthorhombic crystals, which contain 3 monomers of MsCI4 in the asymmetric unit (ASU), were solved on the basis of the MsCI4•thalidomide coordinates 4V2Y; the other two structures were solved by molecular replacement with MOLREP [17], locating one monomer of MsCI4 in ASU”