X-ray Laue Diffraction from Protein Crystals

Moffat, Keith; Szebenyi, Doletha M. E.; Bilderback, Donald H.

doi:10.1126/science.223.4643.1423

Cited by 153 publications

(61 citation statements)

References 12 publications

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“…Bordas, Munro & Glazer (1976) showed that structure-factor amplitudes could be obtained from white-radiation fibre-diffraction studies of collagen and that biological materials could survive exposures to white synchrotron radiation. This lead to trials with protein crystals (Moffat, Szebenyi & Bilderback, 1984;Helliwell, 1984Helliwell, , 1985Hajdu & Stuart, 1985;Hajdu et al, 1986;Moffat, Bilderback, Schildkamp & Volz, 1986) which finally began to yield structural information from both protein and virus crystals (Hajdu et al, , 1989Farber, Machin, Almo, Petsko & Hajdu, 1988;Campbell et al, 1990;Sclichting et al, 1990;Almo, © 1992 International Union of Crystallography . In these studies Laue data have been used in conjunction with difference-Fourier techniques where the initial structure of the protein of interest is available.…”

Section: Introductionmentioning

confidence: 99%

Structure determination of turkey egg-white lysozyme using Laue diffraction data

Howell

Almo²,

Parsons³

et al. 1992

Acta Crystallogr Sect B

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The three-dimensional structure of turkey egg-white lysozyme (TEWL) has been solved and refined at 2.5 A~ resolution using X-ray data collected by the Laue method. This is the first protein structure determination undertaken using Laue diffraction data. A re-examination of the existing structure of TEWL was necessary when attempts to refine an atomic model based on the C,~ positions in the Protein Data Bank (entry 1LZ2) failed. The correct orientation and position of the turkey lysozyme molecules within the crystallographic unit cell were determined by molecular replacement using a refined model of the homologous hen egg-white lysozyme crystal structure. After modification of the model to reflect the differences in amino-acid sequence between the chicken and turkey enzymes, the structure was subjected to crystallographic refinement using the simulated-annealing refinement technique and conventional least-squares refinement. This yielded a final residual of R = 20.7%. This crystal form is of potential interest for time-resolved crystallographic studies since the amino-acid residues involved in

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Section: Introductionmentioning

confidence: 99%

Structure determination of turkey egg-white lysozyme using Laue diffraction data

Howell

Almo²,

Parsons³

et al. 1992

Acta Crystallogr Sect B

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“…Photo-sensitive proteins fall into this category. The fastest X-ray diffraction exposures possible arise from use of the full polychromatic SR X-ray beam where diffraction reflections are integrated over wavelength (the Laue method) (Moffat et al 1984;Helliwell, 1985;Hajdu et al 1987) rather than by rotation of the crystal (as in monochromatic methods). By use of the point-focused white X-ray beam on the high brilliance wiggler/undulator beamline 3 at ESRF in Grenoble, Laue exposures from a myoglobin protein crystal have been recorded from just one electron bunch orbiting the synchrotron ring (Bourgeois et al 1996).…”

Section: Io Dynamical Studies Of Proteins In Crystalsmentioning

confidence: 99%

Trends and Challenges in Experimental Macromolecular Crystallography

Chayen

Boggon

Cassetta

et al. 1996

Quart. Rev. Biophys.

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Macromolecular X-ray crystallography underpins the vigorous field of structural molecular biology having yielded many protein, nucleic acid and virus structures in fine detail. The understanding of the recognition by these macromolecules, as receptors, of their cognate ligands involves the detailed study of the structural chemistry of their molecular interactions. Also these structural details underpin the rational design of novel inhibitors in modern drug discovery in the pharmaceutical industry. Moreover, from such structures the functional details can be inferred, such as the biological chemistry of enzyme reactivity. There is then a vast number and range of types of biological macromolecules that potentially could be studied. The completion of the protein primary sequencing of the yeast genome, and the human genome sequencing project comprising some 105 proteins that is underway, raises expectations for equivalent three dimensional structural databases.

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“…Firstly, where there is a congestion of diffraction spots: (i) building on the protein crystal Laue initiative of Moffat et al (1984) a broader bandpass Laue diffraction pattern ('white beam') approach has been pursued by Helliwell (1984Helliwell ( , 1985 (for a recent overview, see Nieh et al, 1999). The Laue approach, in the narrow bandpass exposition, has more recently become relevant for neutron protein data collection at the Institut Laue Langevin with its Laue diffractometer ('LADI'); see Fig.…”

Section: Experiments Where Good Crystal Perfection Has Been Identifiementioning

confidence: 99%

Protein crystal perfection and its application

Helliwell

2005

Acta Crystallogr D Biol Cryst

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Knowledge of protein crystal perfection in theory and practice is reviewed. X-ray methods of assessing perfection such as mosaicity, topography and reciprocal-space mapping are described. X-ray diffraction physics applications of protein crystals such as in Laue geometry, the large-angle oscillation technique and forming polychromatic profiles across diffraction spots are covered. Cryo-and room-temperature cases are discussed including in X-ray and neutron protein crystallography. Experience of freezing very large crystals, which are commonly used today in neutron protein crystallography, is highlighted.

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X-ray Laue Diffraction from Protein Crystals

Cited by 153 publications

References 12 publications

Structure determination of turkey egg-white lysozyme using Laue diffraction data

Structure determination of turkey egg-white lysozyme using Laue diffraction data

Trends and Challenges in Experimental Macromolecular Crystallography

Protein crystal perfection and its application

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