değerlendirme şakacı Gevşek rwork rfree gap Becks ücret taahhüt
High-Brightness Self-seeded X-ray Free Electron Laser to Precisely Map Macromolecular Structure
Data collection and model refinement statistics | Download Table
Crystallographic Structure Validation - Phenix
Better models by discarding data?
Statistics for x-ray structure determination | Download Table
Data collection and refinement statistics | Download Table
Better models by discarding data?
Data collection and refinement statistics | Download Table
X-ray crystallography–based structural elucidation of enzyme-bound intermediates along the 1‑deoxy‑d‑xylulose 5-phosphat
A description of the structural determination procedures of a gap junction channel at 3.5 Å resolution – topic of research paper in Chemical sciences. Download scholarly article PDF and read for free
Ultrasonic acoustic levitation for fast frame rate X-ray protein crystallography at room temperature | Scientific Reports
Use of knowledge-based restraints in phenix.refine to improve macromolecular refinement at low resolution
Tristan Croll on Twitter: "Some more fun with ISOLDE's adaptive restraints (testing for stability before releasing the official 1.0b5, as much as anything). Today I picked on 1z0v, a 3A crystal from
Tristan Croll on Twitter: "Some more fun with ISOLDE's adaptive restraints (testing for stability before releasing the official 1.0b5, as much as anything). Today I picked on 1z0v, a 3A crystal from
How to reduce large gap between R work and R free ?
Data collection and refinement statistics. | Download Table
Data quality
Tristan Croll on Twitter: "Well... remember what refinement is doing. Essentially, it's trying to make your model look as much like your data as it can, subject to the restraints you provide.
Macromolecular refinement of X-ray and cryo-electron microscopy structures with Phenix / OPLS3e for improved structure and ligand quality | bioRxiv
AutoBusterExample1osgBasicNCS - Kwiki
Rfree and the Rfree ratio
Covid19ReRefineTake1 - Kwiki
Crystals | Free Full-Text | Resolution Dependence of an Ab Initio Phasing Method in Protein X-ray Crystallography | HTML