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5. The crystal structure of human procathepsin K

Author

LaLonde, Judith M., Zhao, Baoquang, Janson, Cheryl A., D'Alessio, Karla J., McQueney, Michael S., Debouck, Christine M., Orsini, Michael J., and Smith, Ward W.

Subjects
Cysteine -- Research, Proteases -- Research, Escherichia coli -- Research, Biological sciences, Chemistry
Abstract

A study was conducted to analyze the crystal structure of procathepsin K, a cysteine protease found in human osteoclasts. Procathepsin K was expressed in Escherichia coli and purified from inclusion bodies. Crystallization trials were then carried out using the hanging drop vapor diffusion technique. Results indicated that the structure of procathepsin K correlated with the molecular basis of inhibition by the propeptide area of the molecule.

Published
1999

6. Design of potent and selective human cathepsin K inhibitors that span the active site

Author

Thompson, Scott K., Halbert, Stacie M., Bossard, Mary J., Tomaszek, Thaddeus A., Levy, Mark A., Zhao, Baoguang, Smith, Ward W., Abdel-Meguid, Sherin S., Janson, Cheryl A., D'Alessio, Karla J., McQueney, Michael S., Amegadzie, Bernard Y., Hanning, Charles R., DesJarlais, Renee L., Briand, Jacques, Sarkar, Susanta K., Huddleston, Michael J., Ijames, Carl F., Carr, Steven A., Garnes, Keith T., Shu, Art, Heys, J. Richard, Bradbeer, Jeremy, Zembryki, Denise, Lee-Rykaczewski, Liz, James, Ian E., Lark, Michael W., Drake, Fred H., Gowen, Maxine, Gleason, John G., and Veber, Daniel F.

Subjects
Cysteine -- Physiological aspects, Enzyme inhibitors -- Research, Nuclear magnetic resonance spectroscopy -- Usage, Proteases -- Physiological aspects, X-ray crystallography -- Usage, Science and technology
Abstract

Potent and selective active-site-spanning inhibitors have been designed for cathepsin K, a cysteine protease unique to osteoclasts. They act by mechanisms that involve tight binding intermediates, potentially on a hydrolytic pathway. X-ray crystallographic, MS, NMR spectroscopic, and kinetic studies of the mechanisms of inhibition indicate that different intermediates or transition states are being represented that are dependent on the conditions of measurement and the specific groups flanking the carbonyl in the inhibitor. The species observed crystallographically are most consistent with tetrahedral intermediates that may be close approximations of those that occur during substrate hydrolysis. Initial kinetic studies suggest the possibility of irreversible and reversible active-site modification. Representative inhibitors have demonstrated antiresorptive activity both in vitro and in vivo and therefore are promising leads for therapeutic agents for the treatment of osteoporosis. Expansion of these inhibitor concepts can be envisioned for the many other cysteine proteases implicated for therapeutic intervention.

Published
1997

7. Active site cavity of herpesvirus proteases revealed by the crystal structure of herpes simplex virus protease/inhibitor complex

Author

Hoog, Susan S., Smith, Ward W., Qui, Xiayang, Janson, Cheryl A., Hellmig, Brian, McQueney, Michael S., O'Donnell, Kevin, O'Shannessy, Daniel, DiLelli, Anthony G., Debouck, Christine, and Abdel-Meguid, Sherin S.

Subjects
Binding sites (Biochemistry) -- Research, Herpes simplex virus -- Research, Biological sciences, Chemistry
Abstract

The covalent inhibitor diispropyl phosphate (DIP) assists in improving delineation of the enzyme active site cavity when studying the crystal structures of the herpes simplex virus proteases. It was established that the overall structure of the HSV-2 protease monomer is similar to that of the structures of CMV and VZV proteases. It is made up of a seven-stranded beta-barrel with seven alpha-helixes. The active site cavity of HSV-2 protease is situated in a shallow groove along the beta-barrel surface.

Published
1997

8. Unique fold and active site in cytomegalovirus protease

Author

Qiu, Xiayang, Culp, Jeffrey S., DiLella, Anthony G., Hellmig, Brian, Hoog, Susan S., Janson, Cheryl A., Smith, Ward W., and Abdel-Meguid, Sherin S.

Subjects
Cytomegaloviruses -- Physiological aspects, Proteases -- Research, Molecular structure -- Observations, Environmental issues, Science and technology, Zoology and wildlife conservation
Abstract

The crystal structure of human cytomegalovirus (CMV) protease at 2.5 resolution shows that this serine protease has a catalytic triad consisting of histidine as a third member. The fold and catalytic site are different from those in other serine proteases. Analysis also reveals a characteristic dimer interface that is important for the protease activity. Human CMV protease is a pathogen that can cause fatal infections in congenitally infected infants, immunocompromised individuals and transplant patients.

Published
1996

9. Rational Approaches to Inhibition of Human Osteoclast Cathepsin K and Treatment of Osteoporosis

Author

Abdel-Meguid, Sherin S., primary, Zhao, Baoguang, additional, Smith, Ward W., additional, Hanson, Cheryl A., additional, LaLonde, Judith, additional, Carr, Thomas, additional, D'Alessio, Karla, additional, McQueney, Michael S., additional, Oh, H.-J., additional, Thompson, Scott K., additional, Veber, Daniel F., additional, and Yamashita, Dennis S., additional

Published
1999
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10. Matrilysin-inhibitor complexes: common themes among metalloproteases

Author

Browner, Michelle F., Smith, Ward W., and Castelhano, Arlindo L.

Subjects
Metalloenzymes -- Research, Enzymes -- Structure-activity relationship, Enzyme kinetics -- Research, Catalysis -- Research, Biological sciences, Chemistry
Abstract

The first X-ray crystal structures of human matrilysin in complex with several different inhibitors are reported. Matrilysin is the smallest member of matrix metalloproteases, a family of enzymes that have important functions in the physiological and pathological degradation of the extracellular matrix and which all need zinc for catalytic activity. These X-ray crystal structures provide detailed information on how each functional group interacts with the catalytic zinc, thus offering a framework for the understanding of the catalytic mechanism of other enzymes from the same family.

Published
1995

11. Structure of human rhinovirus 3C protease reveals a trypsin-like polypeptide fold, RNA-binding site, and means for cleaving precursor polyprotein

Author

Matthews, David A., Smith, Ward W., Ferre, Rose Ann, Condon, Brad, Budahazi, Gregg, Sisson, Wes, Villafranca, J.E., Janson, Cheryl A., McElroy, H.E., Gribskov, C.L., and Worland, Stephen

Subjects
Rhinoviruses -- Genetic aspects, Protein folding -- Research, Biological sciences
Abstract

The structure of human rhinovirus-14 3C protease (3Cpro) discloses folds constituting two topologically equivalent six-stranded beta barrels and suggests means for 3CD polyprotein cleavage. Functions of 3Cpro include providing a binding site for RNA binding with catalytic residues. 3Cpro is akin to trypsin-like serine protease in forming folds.

Published
1994

16. Use of X-ray co-crystal structures and molecular modeling to design potent and selective non-peptide inhibitors of cathepsin K

Author

DesJarlais, Renee L., Yamashita, Dennis S., Oh, Hye-Ja, Uzinskas, Irene N., Erhard, Karl F., Allen, Andrew C., Haltiwanger, R. Curtis, Zhao, Baoguang, Smith, Ward W., Abdel-Meguid, Sherin S., D'Alessio, Karla, Janson, Cheryl A., McQueney, Michael S., Tomaszek, Thaddeus A., Levy, Mark A., and Veber, Daniel F.

Subjects
Protease inhibitors -- Design and construction, Chemical inhibitors -- Design and construction, Chemistry
Abstract

Studies to discover selective inhibitors of cysteine protease Cathepsin K have resulted in the discovery of several innovative classes of cysteine protease inhibitors. A study was conducted where two Cbz-Leu mimetics were designed in the context of cathepsin K binding by the 1,3-bis(acylamino)-2-propane class of inhibitors. One mimetic group can replace the Cbz-Leu on the prime but not unprime side and the latter can replace the Cbz-Leu on the unprime side of the active site.

Published
1998

17. Structure and design of potent and selective Cathepsin K inhibitors

Author

Yamashita, Dennis S., Smith, Ward W., Zhao, Baoguang, Janson, Cheryl A., Tomaszek, Thaddeus A., Bossard, Mary J., Levy, Mark A., Oh, Hye-Ja, Carr, Thomas J., Thompson, Scott K., Ijames, Carl F., Carr, Steven A., McQueney, Michael, D'Alessio, Karla J., Amegadzie, Bernard Y., Hanning, Charles R., Abdel-Meguid, Sherin, DesJarlais, Renee L., Gleason, John G., and Veber, Daniel F.

Subjects
Cysteine proteinases -- Research, Chemistry
Abstract

It has been possible to design selective, 'quiescent', reversible, inhibitors of Cathepsin K based on a poorly electrophilic 1,3-bis(acylamino)-2-propanone scaffold. This approach has considerable potential for further applications, given the extensive range of therapeutic potential predicted for inhibitors of cysteine proteases. Further research will look at potential substrate-like binding interactions on both the primed and unprimed sides of the active site of other unusual cystein proteases.

Published
1997

18. Structure of the semiquinone form of flavodoxin from Clostridium MP Extension of 1.8 A resolution and some comparisons with the oxidized state.

Author

Biophysics Research Division and Department of Biological Chemistry University of Michigan, Ann Arbor, Mich. 48109, U.S.A., Smith, Ward W., Burnett, Roger M., Darling, George D., Ludwig, Martha L., Biophysics Research Division and Department of Biological Chemistry University of Michigan, Ann Arbor, Mich. 48109, U.S.A., Smith, Ward W., Burnett, Roger M., Darling, George D., and Ludwig, Martha L.

Abstract

As part of a series of comparisons of the structures of the three oxidation states of flavodoxin from Clostridium MP, phases for the semiquinono form were determined to 2.0 A resolution by isomorphous replacement (m> = 0.725). Subsequently, the structure was refined at 1.8 A resolution by a combination of difference Fourier, real space and reciprocal space methods. After refining to an R of 0.194, we explored the conformation of the FMN binding site by real space refinement versus maps with Fourier coefficients of the form (2|Fo|- |Fc|) exp (i[alpha]c). To minimize bias in the fitting, groups of atoms were systematically omitted from the structure factors used in computation of the (2|Fo - |Fc|) maps. One-electron reduction of oxidized flavodoxin is accompanied by several changes at the FMN binding site: the conformation of residues in the reverse bend formed by Met56-Gly57-Asp58-Glu59 differs in the crystal structures of the oxidized and semiquinone species; further, backbone atoms in residues 55 and 89 shift by more than 0.5 A and the indole ring of Trp90 undergoes a significant displacement. The orientation of the peptide unit connecting Gly57 and Asp58 is consistent with the presence of a hydrogen bond between the carbonyl oxygen of Gly57 and the flavin N(5) in flavodoxin semiquinone. No equivalent bond is found in oxidized flavodoxin. In both the oxidized and semiquinone species of clostridial flavodoxin, the isoalloxazine ring is essentially planar : the bending angles about N(5)---N(10) are ~2.5 [deg] for the semiquinone structure and ~0 [deg] in oxidized flavodoxin. The intensity changes resulting from the oxidized agsemiquinone conversion (RI = 0.33) arise in part from changes in molecular packing. Intermolecular contacts, including neighbors of the prosthetic group, are altered in the repacking. Maps or models of the two oxidation states can be brought into approximate coincidence by a rigid body motion. The required transformation, determined for the is

Published
2006

19. Crystallographic characterization of flavodoxin from Anacystis nidulans

Author

Department of Biological Chemistry University of Michigan Medical School, Ann Arbor, Mich. 48105, U.S.A.; Department of Chemistry University of Michigan, Ann Arbor, Mich. 48105, U.S.A.; Biophysics Research Division, University of Michigan, Ann Arbor, Mich. 48105, U.S.A., Chemistry Division, Argonne National Laboratory, Argonne, Ill., U.S.A., Smith, Ward W., Entsch, Barrie, Ludwig, Martha L., Nordman, C.E., Crespi, Henry L., Department of Biological Chemistry University of Michigan Medical School, Ann Arbor, Mich. 48105, U.S.A.; Department of Chemistry University of Michigan, Ann Arbor, Mich. 48105, U.S.A.; Biophysics Research Division, University of Michigan, Ann Arbor, Mich. 48105, U.S.A., Chemistry Division, Argonne National Laboratory, Argonne, Ill., U.S.A., Smith, Ward W., Entsch, Barrie, Ludwig, Martha L., Nordman, C.E., and Crespi, Henry L.

Abstract

Flavodoxin isolated from the blue-green alga, Anacystis nidulans, crystallizes from ammonium sulfate in space group P212121, with a = 57.08 A, B = 69.24 A and C = 45.55 A. The diffraction patterns extend to a resolution of at least 1.8 A. Reduction of the flavin mononucleotide in the crystalline protein, to either the semi-quinone or fully reduced (hydroquinone) state, results in minimal changes in cell dimensions and diffracted intensities. The higher molecular weight (19,000 to 20,000) and spectral properties of the A. nidulans protein, along with the near-isomorphism of crystals of the three oxidation states, distinguish this crystalline flavodoxin from the corresponding proteins of Clostaridium MP and Desulfovibrio vulgaris, whose three-dimensional structures are known. In contrast to Clostridium flavodoxins, but like the D. vulgaris protein, A. nidulans flavodoxin is capable of binding riboflavin in place of flavin mononucleotide (Ka = 2 x 106m-1).

Published
2006

21. Highly Potent Inhibitors of Methionine Aminopeptidase-2 Based on a 1,2,4-Triazole Pharmacophore

Author

Marino,, Joseph P., primary, Fisher, Paul W., additional, Hofmann, Glenn A., additional, Kirkpatrick, Robert B., additional, Janson, Cheryl A., additional, Johnson, Randall K., additional, Ma, Chun, additional, Mattern, Michael, additional, Meek, Thomas D., additional, Ryan, M. Dominic, additional, Schulz, Christina, additional, Smith, Ward W., additional, Tew, David G., additional, Tomazek, Thaddeus A., additional, Veber, Daniel F., additional, Xiong, Wenfang C., additional, Yamamoto, Yuuichi, additional, Yamashita, Keizo, additional, Yang, Guang, additional, and Thompson, Scott K., additional

Published
2007
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22. Structure Activity Relationships of 5-, 6-, and 7-Methyl-Substituted Azepan-3-one Cathepsin K Inhibitors

Author

Yamashita, Dennis S., primary, Marquis, Robert W., additional, Xie, Ren, additional, Nidamarthy, Sirishkumar D., additional, Oh, Hye-Ja, additional, Jeong, Jae U., additional, Erhard, Karl F., additional, Ward, Keith W., additional, Roethke, Theresa J., additional, Smith, Brian R., additional, Cheng, H-Y., additional, Geng, Xiaoliu, additional, Lin, Fan, additional, Offen, Priscilla H., additional, Wang, Bing, additional, Nevins, Neysa, additional, Head, Martha S., additional, Haltiwanger, R. Curtis, additional, Narducci Sarjeant, Amy A., additional, Liable-Sands, Louise M., additional, Zhao, Baoguang, additional, Smith, Ward W., additional, Janson, Cheryl A., additional, Gao, Enoch, additional, Tomaszek, Thaddeus, additional, McQueney, Michael, additional, James, Ian E., additional, Gress, Catherine J., additional, Zembryki, Denise L., additional, Lark, Michael W., additional, and Veber, Daniel F., additional

Published
2006
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24. 4-Aryl-1,2,3-triazole: A Novel Template for a Reversible Methionine Aminopeptidase 2 Inhibitor, Optimized To Inhibit Angiogenesis in Vivo

Author

Kallander, Lara S., primary, Lu, Qing, additional, Chen, Wenfang, additional, Tomaszek, Thaddeus, additional, Yang, Guang, additional, Tew, David, additional, Meek, Thomas D., additional, Hofmann, Glenn A., additional, Schulz-Pritchard, Christina K., additional, Smith, Ward W., additional, Janson, Cheryl A., additional, Ryan, M. Dominic, additional, Zhang, Gui-Feng, additional, Johanson, Kyung O., additional, Kirkpatrick, Robert B., additional, Ho, Thau F., additional, Fisher, Paul W., additional, Mattern, Michael R., additional, Johnson, Randall K., additional, Hansbury, Michael J., additional, Winkler, James D., additional, Ward, Keith W., additional, Veber, Daniel F., additional, and Thompson, Scott K., additional

Published
2005
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26. Crystal structure of Staphylococcus aureus tyrosyl‐tRNA synthetase in complex with a class of potent and specific inhibitors

Author

Qiu, Xiayang, primary, Janson, Cheryl A., additional, Smith, Ward W., additional, Green, Susan M., additional, McDevitt, Patrick, additional, Johanson, Kyung, additional, Carter, Paul, additional, Hibbs, Martin, additional, Lewis, Ceri, additional, Chalker, Alison, additional, Fosberry, Andrew, additional, Lalonde, Judith, additional, Berge, John, additional, Brown, Pamela, additional, Houge‐Frydrych, Catherine S.V., additional, and Jarvest, Richard L., additional

Published
2001
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27. Cyclic Ketone Inhibitors of the Cysteine Protease Cathepsin K

Author

Marquis, Robert W., primary, Ru, Yu, additional, Zeng, Jin, additional, Trout, Robert E. Lee, additional, LoCastro, Stephen M., additional, Gribble, Andrew D., additional, Witherington, Jason, additional, Fenwick, Ashley E., additional, Garnier, Benedicte, additional, Tomaszek, Thaddeus, additional, Tew, David, additional, Hemling, Mark E., additional, Quinn, Chad J., additional, Smith, Ward W., additional, Zhao, Baoguang, additional, McQueney, Michael S., additional, Janson, Cheryl A., additional, D'Alessio, Karla, additional, and Veber, Daniel F., additional

Published
2001
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29. The Crystal Structure of Human Procathepsin K

Author

LaLonde, Judith M., primary, Zhao, Baoguang, additional, Janson, Cheryl A., additional, D'Alessio, Karla J., additional, McQueney, Michael S., additional, Orsini, Michael J., additional, Debouck, Christine M., additional, and Smith, Ward W., additional

Published
1998
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30. Use of Papain as a Model for the Structure-Based Design of Cathepsin K Inhibitors: Crystal Structures of Two Papain−Inhibitor Complexes Demonstrate Binding to S‘-Subsites

Author

LaLonde, Judith M., primary, Zhao, Baoguang, additional, Smith, Ward W., additional, Janson, Cheryl A., additional, DesJarlais, Renee L., additional, Tomaszek, Thaddeus A., additional, Carr, Thomas J., additional, Thompson, Scott K., additional, Oh, Hye-Ja, additional, Yamashita, Dennis S., additional, Veber, Daniel F., additional, and Abdel-Meguid, Sherin S., additional

Published
1998
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31. Structure-Based Design of Cathepsin K Inhibitors Containing a Benzyloxy-Substituted Benzoyl Peptidomimetic

Author

Thompson, Scott K., primary, Smith, Ward W., additional, Zhao, Baoguang, additional, Halbert, Stacie M., additional, Tomaszek, Thaddeus A., additional, Tew, David G., additional, Levy, Mark A., additional, Janson, Cheryl A., additional, D‘Alessio, Karla J., additional, McQueney, Michael S., additional, Kurdyla, Jeff, additional, Jones, Christopher S., additional, DesJarlais, Renee L., additional, Abdel-Meguid, Sherin S., additional, and Veber, Daniel F., additional

Published
1998
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32. Conformationally Constrained 1,3-Diamino Ketones: A Series of Potent Inhibitors of the Cysteine Protease Cathepsin K

Author

Marquis, Robert W., primary, Yamashita, Dennis S., additional, Ru, Yu, additional, LoCastro, Stephen M., additional, Oh, Hye-Ja, additional, Erhard, Karl F., additional, DesJarlais, Renee L., additional, Head, Martha S., additional, Smith, Ward W., additional, Zhao, Baoguang, additional, Janson, Cheryl A., additional, Abdel-Meguid, Sherin S., additional, Tomaszek, Thaddeus A., additional, Levy, Mark A., additional, and Veber, Daniel F., additional

Published
1998
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33. Crystal structure of human osteoclast cathepsin K complex with E-64

Author

Zhao, Baoguang, primary, Janson, Cheryl A., additional, Amegadzie, Bernard Y., additional, D'Alessio, Karla, additional, Griffin, Charles, additional, Hanning, Charles R., additional, Jones, Christopher, additional, Kurdyla, Jeff, additional, McQueney, Michael, additional, Qiu, Xiayang, additional, Smith, Ward W., additional, and Abdel-Meguid, Sherin S., additional

Published
1997
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34. Structure-Based Design of Substituted Diphenyl Sulfones and Sulfoxides as Lipophilic Inhibitors of Thymidylate Synthase

Author

Jones, Terence R., primary, Webber, Stephen E., additional, Varney, Michael D., additional, Reddy, M. Rami, additional, Lewis, Kathleen K., additional, Kathardekar, Vinit, additional, Mazdiyasni, Hormoz, additional, Deal, Judith, additional, Nguyen, Dzuy, additional, Welsh, Katharine M., additional, Webber, Stephanie, additional, Johnston, Amanda, additional, Matthews, David A., additional, Smith, Ward W., additional, Janson, Cheryl A., additional, Bacquet, Russell J., additional, Howland, Eleanor F., additional, Booth, Carol L. J., additional, Herrmann, Steven M., additional, Ward, Robert W., additional, White, Jennifer, additional, Bartlett, Charlotte A., additional, and Morse, Cathy A., additional

Published
1997
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35. Structure-Based Design of Lipophilic Quinazoline Inhibitors of Thymidylate Synthase

Author

Jones, Terence R., primary, Varney, Michael D., additional, Webber, Stephen E., additional, Lewis, Kathleen K., additional, Marzoni, Gifford P., additional, Palmer, Cindy L., additional, Kathardekar, Vinit, additional, Welsh, Katharine M., additional, Webber, Stephanie, additional, Matthews, David A., additional, Appelt, Krzysztof, additional, Smith, Ward W., additional, Janson, Cheryl A., additional, Villafranca, J. E., additional, Bacquet, Russell J., additional, Howland, Eleanor F., additional, Booth, Carol L. J., additional, Herrmann, Steven M., additional, Ward, Robert W., additional, White, Jennifer, additional, Moomaw, Ellen W., additional, Bartlett, Charlotte A., additional, and Morse, Cathy A., additional

Published
1996
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38. In situ data collection and structure refinement from microcapillary protein crystallization.

Author

Yadav, Maneesh K., Gerdts, Cory J., Sanishvili, Ruslan, Smith, Ward W., Roach, L. Spencer, Ismagilov, Rustem F., Kuhn, Peter, and Stevens, Raymond C.

Subjects
X-rays, CRYSTALLOIDS (Botany), PROTEINS, CAPILLARIES, FLUOROCARBONS, ELECTRON distribution
Abstract

In situ X-ray data collection has the potential to eliminate the challenging task of mounting and cryocooling often fragile protein crystals, reducing a major bottleneck in the structure determination process. An apparatus used to grow protein crystals in capillaries and to compare the background X-ray scattering of the components, including thin-walled glass capillaries against Teflon, and various fluorocarbon oils against each other, is described. Using thaumatin as a test case at 1.8 Å resolution, this study demonstrates that high-resolution electron density maps and refined models can be obtained from in situ diffraction of crystals grown in microcapillaries. [ABSTRACT FROM AUTHOR]

Published
2005
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39. Crystal structure of varicella-zoster virus protease.

Author

Xiayang Qiu, Janson, Cheryl A., Culp, Jeffrey S., Richardson, Susan B., Debouck, Christine, Smith, Ward W., and Abdel-Meguid, Sherin S.

Subjects
VARICELLA-zoster virus, PROTEOLYTIC enzymes
Abstract

Describes the determination of the three-dimensional crystal structure of the serine protease from varicella-zoster virus (VZV). VZV as a causative agent of chickenpox, shingles and postherpetic neuralgia; Overall fold similar to the serine protease from cytomegalovirus (CMV); Protease catalytic triad.

Published
1997
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40. The Structure of the Oxidized Form of Clostridial Flavodoxin at 1.9-A Resolution

Author

Burnett, Roger M., Darling, George D., Kendall, Douglas S., LeQuesne, Mary E., Mayhew, Stephen G., Smith, Ward W., and Ludwig, Martha L.

Abstract

An electron density map of the oxidized form of flavodoxin from Clostridiumstrain MP has been calculated to a resolution of 1.9 A employing isomorphous and anomalous scattering data from two heavy atom derivatives, Smiiiand Aui. In the region from 3.0 to 1.9 A, the largest structure amplitudes (85% of the total | F| s) have been included in the computation. The over-all figure of merit is 0.808. The molecular model resulting from interpretation of this map has a chain length of 138 residues, in accord with the sequence (Tanaka, M., Haniu, M., Yasunobu, K. T., andMayhew, S. G. (1974) J. Biol. Chem.249, 4393–4396). As reported earlier, the molecule possesses a high degree of secondary structure, including a central parallel sheet and four helices. More than 70% of the residues appear to participate in backbone hydrogen bonding. Atomic coordinates, incorporating the sequence data, have been optimized by use of Diamond's model-building program.

Published
1974
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47. The Impact of Cryogenic Specimen Automounters on the Future of Macromolecular Crystallography.

Author

SWEET, ROBERT and SMITH, WARD W.

Subjects
*LOW temperature engineering, *CRYSTALLOGRAPHY, *SYNCHROTRON radiation, *SYNCHROTRON radiation sources, *CONFERENCES & conventions
Abstract

Reports on the highlights of the workshop on the impact of cryogenic specimen automounters on the future of macromolecular crystallography, at the 2005 National Synchrotron Light Source (NSLS) Annual Users' Meeting. Thomas Earnest's description of an automounter system based on pneumatic actuators; Quan Hao's report on a miniature liquid nitrogen pump for filling the sample dewar; Frank Felisaz's description of a robot named SC3, which was developed by the European Molecular Biology Lab.

Published
2005

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