Protein crystal structures: quicker, cheaper approaches

  title={Protein crystal structures: quicker, cheaper approaches},
  author={Douglas M. Collins and F. A. Cotton and E. E. Jun. Hazen and Edgar F. Meyer and Carl N. Morimoto},
  pages={1047 - 1053}
The use of x-ray diffraction methods to study crystals of biological macromolecules dates from 1934, when Bernal and Crowfoot (1) found that the diffraction patterns from crystals of the proteolytic enzyme pepsin were, in Hodgkin's words (2), "rich and full of detail." The potential for revealing the precise molecular structure of protein molecules inherent in such diffraction patterns remained unrealized until 1954, when M. F. Perutz, who had devoted his early career to the effort, showed that… 
Molecular Embodiments and the Body-work of Modeling in Protein Crystallography
This ethnographic study of protein crystallography shows that becoming an expert crystallographer, and so making sense of such intricate objects, requires researchers to draw on their bodies as a resource to learn about, work with, and communicate precise molecular configurations.
Crystal structure of a eukaryotic initiator tRNA
The initial results of the crystal structure determination of a eukaryotic initiator tRNA crystallised from a highly polar aqueous solvent are reported, and its architecture is essentially the same as crystalline yeast tRNAphe, except for a small but significant difference in the position of the anticodon arm.
Density Modification Methods
Macromolecular crystallography is growing rapidly as a tool to image the structure of proteins, nucleic acids and their interactions . In many of these projects, however, MIR (Multiple Isomorphous
Display, manipulation, and simulation of macromolecules
This study emphasizes the availability of an easy to handle and inexpensive means for building, displaying, and manipulating molecules in the study of the interaction of proteins with DNA and RNA.
Interactive computer graphics for bio-stereochemical modelling
The RPMI system which is currently running on the Univac 70 computer, is easily adaptable to any computer, with or without sophisticated graphics hardware, and the availability of an easy to handle and inexpensive means for building, manipulating, and displaying molecules is emphasized.


Crystallographic refinement of the structure of bovine pancreatic trypsin inhibitor at l.5 Å resolution
The model of pancreatic trypsin inhibitor determined by Huber, Kukla, Rtihlmann, Epp & Formanek [Naturwissenschaften (1970). 57, 389-392] was fitted to an electron-density map of 1.9 A resolution
Refinement of the model of a protein: rubredoxin at 1.5 Å resolution
Rubredoxin from Clostridium pasteurianum is an iron sulfur protein of molecular weight ~ 6100. Crystals are grown by salting out from aqueous (NH4)2804 at pH 4. They belong to the trigonal system,
Least‐squares phase refinement. II. High‐resolution phasing of a small protein
A recently described technique for direct least-squares refinement of phases has been successfully applied to the problem of phasing a 1.5 A data set of observed structure-factor magnitudes for C.
A high resolution structure of an inhibitor complex of the extracellular nuclease of Staphylococcus aureus. I. Experimental procedures and chain tracing.
The most significant feature of the nuclease structure is a large pocket which serves as the inhibitor binding site, and the lining of this pocket is revealed to be predominantly neutral or hydrophobic with the exception of several residues which specifically participate in binding the calcium ion and the nucleoside diphosphate.
Energy refinement of hen egg-white lysozyme.
  • M. Levitt
  • Chemistry
    Journal of molecular biology
  • 1974
The extracellular nuclease of Staphylococcus aureus: structures of the native enzyme and an enzyme-inhibitor complex at 4 A resolution.
The pyrimidine ring of the inhibitor fits into a pocket in the enzyme and appears to be parallel to the ring of a tyrosyl residue, but the two structures seem to be identical over most of the molecule.