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D L Wild

Publications and source records attributed to D L Wild.

5 recordsLinked to original sources
PubMed2001

An exponential modeling algorithm for protein structure completion by X-ray crystallography.

An exponential modeling algorithm is developed for protein structure completion by X-ray crystallography and tested on experimental data from a 59-residue protein. An initial noisy difference Fourier map of missing residues of up to half of the protein is transformed by the algorithm into one that allows easy identification of the continuous tube of electron density associated with that polypeptide chain. The method incorporates the paradigm of phase hypothesis generation and cross validation within an automated scheme.

Algorithms↗
PubMed1995

A visual data flow environment for macromolecular crystallographic computing.

This article describes the integration of programs from the widely used CCP4 macromolecular crystallography package into a modern data flow visualization environment (application visualization system [AVS]), which provides a simple graphical user interface, a visual programming paradigm, and a variety of 1-, 2-, and 3-D data visualization tools for the display of graphical information and the results of crystallographic calculations, such as electron density and Patterson maps. The CCP4 suite comprises a number of separate Fortran 77 programs, which communicate via common file formats. Each program is encapsulated into an AVS macro module, and may be linked to others in a data flow network, reflecting the nature of many crystallographic calculations. Named pipes are used to pass input parameters from a graphical user interface to the program module, and also to intercept line printer output, which can be filtered to extract graphical information and significant numerical parameters. These may be passed to downstream modules, permitting calculations to be automated if no user interaction is required, or giving the user the opportunity to make selections in an interactive manner.

Base Sequence↗
PubMed1978

Crystallographic studies on the activity of glycogen phosphorylase b.

High resolution studies on the crystal structure of glycogen phosphorylase b have identified the catalytic site to which the substrate glucose-1-phosphate binds strongly with some local conformational changes. The site is situated 8 A (phosphate-to-phosphate distance) from pyridoxal phosphate, an essential cofactor of all glycogen phosphorylases. The catalytic site is 33 A from the site in the N-terminal portion of the molecule to which adenine nucleotides bind. In contrast to phosphorylase a (the active form of the enzyme which is phosphorylated at Ser 14), the positions of the first 19 residues of phosphorylase b are not well defined.

Adenosine Monophosphate↗