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J. Appl. Cryst.の発刊に際して

良二 上田
- Vol. 12, Iss: 1, pp 1-1
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The article was published on 1970-03-10 and is currently open access. It has received 8159 citations till now.

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A short history of SHELX

TL;DR: This paper could serve as a general literature citation when one or more of the open-source SH ELX programs (and the Bruker AXS version SHELXTL) are employed in the course of a crystal-structure determination.
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The Protein Data Bank

TL;DR: The goals of the PDB are described, the systems in place for data deposition and access, how to obtain further information and plans for the future development of the resource are described.
Journal ArticleDOI

Crystal structure refinement with SHELXL

TL;DR: New features added to the refinement program SHELXL since 2008 are described and explained.
Journal ArticleDOI

Coot: model-building tools for molecular graphics.

TL;DR: CCP4mg is a project that aims to provide a general-purpose tool for structural biologists, providing tools for X-ray structure solution, structure comparison and analysis, and publication-quality graphics.
References
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Journal ArticleDOI

Is it jolly SAD

TL;DR: Examples of phasing macromolecular crystal structures based on single-wavelength anomalous dispersion (SAD) show that this approach is more powerful and may have more general application in structural biology than was anticipated.
Journal ArticleDOI

Extending molecular-replacement solutions with SHELXE

TL;DR: Under favourable circumstances, density modification and polyalanine tracing with SHELXE can be used to improve and validate potential solutions from molecular replacement.
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Structures of the B1 domain of protein L from Peptostreptococcus magnus with a tyrosine to tryptophan substitution

TL;DR: These high-resolution structures of the tryptophan-containing variant provide a reference frame for the analysis of thermodynamic and kinetic data derived from a series of mutational studies of the protein L B1 domain.
Journal ArticleDOI

Structural basis for hijacking siderophore receptors by antimicrobial lasso peptides.

TL;DR: The lasso peptide microcin J25 is known to hijack the siderophore receptor FhuA for initiating internalization and the first structural evidence on the recognition mechanism is provided and biochemical data show that another closely related lasso Peptide cannot interact with F HuA.