CHAINSAW: a program for mutating pdb files used as templates in molecular replacement
By N. Stein. 2008
572 citations recorded by the source corpus.
Subfields: Materials Chemistry, Molecular Biology
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In Materials Chemistry
In Molecular Biology
Citations in the corpus
- Improvement of molecular-replacement models with Sculptor (2011, methodology): “These algorithms have since been implemented in the CCP4 (Winn et al., 2011) programs CHAINSAW (Stein, 2008) and MOLREP (Vagin & Teplyakov, 2010).”
- Overview of the CCP4 suite and current developments (2011, methodology): “The program CHAINSAW (Stein, 2008) takes as input a sequence alignment which relates residues in the search model to residues in the target protein and uses this information to edit the search model appropriately.”
- Structural basis of WLS/Evi-mediated Wnt transport and secretion (2020, methodology): “To build the WNT8A-WLS model we first made threaded a homology model of WNT8A based on the xWnt8 structure (PDB ID 4F0A) using CHAINSAW (Stein, 2008).”
- Using iterative fragment assembly and progressive sequence truncation to facilitate phasing and crystal structure determination of distantly related proteins. (2016, methodology): “The first successful I-TASSER search model has an r.m.s.d. of 1.76 Å and a TM-score of 0.69, while the r.m.s.d. and TM-score of the best of 13 LOMETS search models produced by CHAINSAW and Sculptor are 2.0 Å and 0.62, respectively.”
- Structure-Function Analysis of Heterodimer Formation, Oligomerization, and Receptor Binding of the Staphylococcus aureus Bi-component Toxin LukGH* (2014, methodology): “Chains A and B of Protein Data Bank code 3B07 were processed using Chainsaw (27), and two full octamers were then generated by superimposing them on the 8 dimers in the octameric pores.”
- Structures of bovine, equine and leporine serum albumin. (2012, methodology): “The amino-acid sequence was modified with the program CHAINSAW (Stein, 2008; Schwarzenbacher et al., 2004); the side chains were removed from the model, leaving only the part common to the sequence of the target protein.”
- ISOLDE: a physically realistic environment for model building into low-resolution electron-density maps (2018, methodology): “…built into 3.8 Å resolution cryo-EM density starting from homology models generated from a distantly related archaeal homohexamer using CHAINSAW (Stein, 2008), followed by extensive iterations of manual rebuilding in Coot and refinement with phenix.real_space_refine using Ramachandran and…”