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The application of direct methods and Patterson interpretation to high-resolution native protein data.

Acta crystallographica. Section D, Biological crystallography

Sheldrick GM, Dauter Z, Wilson KS, Hope H, Sieker LC.
PMID: 15299542
Acta Crystallogr D Biol Crystallogr. 1993 Jan 01;49:18-23. doi: 10.1107/S0907444992007364.

Conventional small-molecule methods of solving the phase problem from native data alone, without the use of heavy-atom derivatives, known fragment geometries or anomalous dispersion, have been tested on 0.9 A resolution data for two small proteins: rubredoxin, from Desulfovibrio...

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Sheldrick GM, Dauter Z, Wilson KS, et al. The application of direct methods and Patterson interpretation to high-resolution native protein data. Acta Crystallogr D Biol Crystallogr. 1993;49:18-23doi: 10.1107/S0907444992007364.
Sheldrick, G. M., Dauter, Z., Wilson, K. S., Hope, H., & Sieker, L. C. (1993). The application of direct methods and Patterson interpretation to high-resolution native protein data. Acta crystallographica. Section D, Biological crystallography, 4918-23. https://doi.org/10.1107/S0907444992007364
Sheldrick, G M, et al. "The application of direct methods and Patterson interpretation to high-resolution native protein data." Acta crystallographica. Section D, Biological crystallography vol. 49 (1993): 18-23. doi: https://doi.org/10.1107/S0907444992007364
Sheldrick GM, Dauter Z, Wilson KS, Hope H, Sieker LC. The application of direct methods and Patterson interpretation to high-resolution native protein data. Acta Crystallogr D Biol Crystallogr. 1993 Jan 01;49:18-23. doi: 10.1107/S0907444992007364. PMID: 15299542.
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Refined structure of Cu-substituted alcohol dehydrogenase at 2.1 A resolution.

Acta crystallographica. Section D, Biological crystallography

Al-Karadaghi S, Cedergren-Zeppezauer ES, Dauter Z, Wilson KS.
PMID: 15299812
Acta Crystallogr D Biol Crystallogr. 1995 Sep 01;51:805-13. doi: 10.1107/S090744499500045X.

Liver alcohol dehydrogenase (LADH) is a Zn(II)-dependent dimeric enzyme. LADH with the active-site Zn(II) substituted by Cu(II) resembles blue (type I) copper proteins by its spectroscopic characteristics. In this work we present the X-ray structure of the active site...

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Al-Karadaghi S, Cedergren-Zeppezauer ES, Dauter Z, et al. Refined structure of Cu-substituted alcohol dehydrogenase at 2.1 A resolution. Acta Crystallogr D Biol Crystallogr. 1995;51:805-13doi: 10.1107/S090744499500045X.
Al-Karadaghi, S., Cedergren-Zeppezauer, E. S., Dauter, Z., & Wilson, K. S. (1995). Refined structure of Cu-substituted alcohol dehydrogenase at 2.1 A resolution. Acta crystallographica. Section D, Biological crystallography, 51805-13. https://doi.org/10.1107/S090744499500045X
Al-Karadaghi, S, et al. "Refined structure of Cu-substituted alcohol dehydrogenase at 2.1 A resolution." Acta crystallographica. Section D, Biological crystallography vol. 51 (1995): 805-13. doi: https://doi.org/10.1107/S090744499500045X
Al-Karadaghi S, Cedergren-Zeppezauer ES, Dauter Z, Wilson KS. Refined structure of Cu-substituted alcohol dehydrogenase at 2.1 A resolution. Acta Crystallogr D Biol Crystallogr. 1995 Sep 01;51:805-13. doi: 10.1107/S090744499500045X. PMID: 15299812.
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Crystallographic analyses of an active HIV-1 ribonuclease H domain show structural features that distinguish it from the inactive form.

Acta crystallographica. Section D, Biological crystallography

Chattopadhyay D, Finzel BC, Munson SH, Evans DB, Sharma SK, Strakalaitus NA, Brunner DP, Eckenrode FM, Dauter Z, Betzel C, Einspahr HM.
PMID: 15299518
Acta Crystallogr D Biol Crystallogr. 1993 Jul 01;49:423-7. doi: 10.1107/S0907444993002409.

. An active recombinant preparation of the carboxy-terminal ribonuclease H (RNase H) domain of HIV-I reverse transcriptase has produced crystals of several different forms, including a trigonal prism form (P3(1); a = b = 52.03, c = 113.9 A...

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Chattopadhyay D, Finzel BC, Munson SH, et al. Crystallographic analyses of an active HIV-1 ribonuclease H domain show structural features that distinguish it from the inactive form. Acta Crystallogr D Biol Crystallogr. 1993;49:423-7doi: 10.1107/S0907444993002409.
Chattopadhyay, D., Finzel, B. C., Munson, S. H., Evans, D. B., Sharma, S. K., Strakalaitus, N. A., Brunner, D. P., Eckenrode, F. M., Dauter, Z., Betzel, C., & Einspahr, H. M. (1993). Crystallographic analyses of an active HIV-1 ribonuclease H domain show structural features that distinguish it from the inactive form. Acta crystallographica. Section D, Biological crystallography, 49423-7. https://doi.org/10.1107/S0907444993002409
Chattopadhyay, D, et al. "Crystallographic analyses of an active HIV-1 ribonuclease H domain show structural features that distinguish it from the inactive form." Acta crystallographica. Section D, Biological crystallography vol. 49 (1993): 423-7. doi: https://doi.org/10.1107/S0907444993002409
Chattopadhyay D, Finzel BC, Munson SH, Evans DB, Sharma SK, Strakalaitus NA, Brunner DP, Eckenrode FM, Dauter Z, Betzel C, Einspahr HM. Crystallographic analyses of an active HIV-1 ribonuclease H domain show structural features that distinguish it from the inactive form. Acta Crystallogr D Biol Crystallogr. 1993 Jul 01;49:423-7. doi: 10.1107/S0907444993002409. PMID: 15299518.
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Compressibility of lysozyme protein crystals by X-ray diffraction.

Acta crystallographica. Section D, Biological crystallography

Katrusiak A, Dauter Z.
PMID: 15299694
Acta Crystallogr D Biol Crystallogr. 1996 May 01;52:607-8. doi: 10.1107/S0907444996000431.

Single-crystal high-pressure X-ray diffraction studies on the protein crystals of orthorhombic and tetragonal hen egg-white lysozyme polymorphs were carried out using a Merrill-Bassett diamond-anvil cell, image-plate detector and synchrotron radiation. The orthorhombic crystal has been squeezed to 85.5% of...

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Katrusiak A, Dauter Z. Compressibility of lysozyme protein crystals by X-ray diffraction. Acta Crystallogr D Biol Crystallogr. 1996;52:607-8doi: 10.1107/S0907444996000431.
Katrusiak, A., & Dauter, Z. (1996). Compressibility of lysozyme protein crystals by X-ray diffraction. Acta crystallographica. Section D, Biological crystallography, 52607-8. https://doi.org/10.1107/S0907444996000431
Katrusiak, A, and Dauter, Z. "Compressibility of lysozyme protein crystals by X-ray diffraction." Acta crystallographica. Section D, Biological crystallography vol. 52 (1996): 607-8. doi: https://doi.org/10.1107/S0907444996000431
Katrusiak A, Dauter Z. Compressibility of lysozyme protein crystals by X-ray diffraction. Acta Crystallogr D Biol Crystallogr. 1996 May 01;52:607-8. doi: 10.1107/S0907444996000431. PMID: 15299694.
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Ribonuclease from Streptomyces aureofaciens at atomic resolution.

Acta crystallographica. Section D, Biological crystallography

Sevcik J, Dauter Z, Lamzin VS, Wilson KS.
PMID: 15299705
Acta Crystallogr D Biol Crystallogr. 1996 Mar 01;52:327-44. doi: 10.1107/S0907444995007669.

Crystals of ribonuclease from Streptomyces aureofaciens diffract to atomic resolution at room temperature. Using synchrotron radiation and an imaging-plate scanner, X-ray data have been recorded to 1.20 A resolution from a crystal of native enzyme and to 1.15 A...

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Sevcik J, Dauter Z, Lamzin VS, et al. Ribonuclease from Streptomyces aureofaciens at atomic resolution. Acta Crystallogr D Biol Crystallogr. 1996;52:327-44doi: 10.1107/S0907444995007669.
Sevcik, J., Dauter, Z., Lamzin, V. S., & Wilson, K. S. (1996). Ribonuclease from Streptomyces aureofaciens at atomic resolution. Acta crystallographica. Section D, Biological crystallography, 52327-44. https://doi.org/10.1107/S0907444995007669
Sevcik, J, et al. "Ribonuclease from Streptomyces aureofaciens at atomic resolution." Acta crystallographica. Section D, Biological crystallography vol. 52 (1996): 327-44. doi: https://doi.org/10.1107/S0907444995007669
Sevcik J, Dauter Z, Lamzin VS, Wilson KS. Ribonuclease from Streptomyces aureofaciens at atomic resolution. Acta Crystallogr D Biol Crystallogr. 1996 Mar 01;52:327-44. doi: 10.1107/S0907444995007669. PMID: 15299705.
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Purification, crystallization and preliminary X-ray crystallographic analysis of lactoperoxidase from buffalo milk.

Acta crystallographica. Section D, Biological crystallography

Kumar R, Bhatia KL, Dauter Z, Betzel C, Singh TP.
PMID: 15299785
Acta Crystallogr D Biol Crystallogr. 1995 Nov 01;51:1094-6. doi: 10.1107/S0907444995004422.

The lactoperoxidase was prepared from buffalo milk and purified using CM-Sephadex C-50 and Sephadex G-100. The activity of the enzyme was measured using 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) diammonium salt as a chromogenic substrate at pH 6.0. The purified protein was crystallized...

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Kumar R, Bhatia KL, Dauter Z, et al. Purification, crystallization and preliminary X-ray crystallographic analysis of lactoperoxidase from buffalo milk. Acta Crystallogr D Biol Crystallogr. 1995;51:1094-6doi: 10.1107/S0907444995004422.
Kumar, R., Bhatia, K. L., Dauter, Z., Betzel, C., & Singh, T. P. (1995). Purification, crystallization and preliminary X-ray crystallographic analysis of lactoperoxidase from buffalo milk. Acta crystallographica. Section D, Biological crystallography, 511094-6. https://doi.org/10.1107/S0907444995004422
Kumar, R, et al. "Purification, crystallization and preliminary X-ray crystallographic analysis of lactoperoxidase from buffalo milk." Acta crystallographica. Section D, Biological crystallography vol. 51 (1995): 1094-6. doi: https://doi.org/10.1107/S0907444995004422
Kumar R, Bhatia KL, Dauter Z, Betzel C, Singh TP. Purification, crystallization and preliminary X-ray crystallographic analysis of lactoperoxidase from buffalo milk. Acta Crystallogr D Biol Crystallogr. 1995 Nov 01;51:1094-6. doi: 10.1107/S0907444995004422. PMID: 15299785.
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[Günter Stüttgen on his 60th birthday].

Zeitschrift fur Hautkrankheiten

Goerz G.
PMID: 366938
Z Hautkr. 1979 Jan 15;54(2):39-41.

No abstract available.

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Goerz G. Günter Stüttgen zum 60. Geburtstag. [Günter Stüttgen on his 60th birthday]. Z Hautkr. 1979;54(2):39-41
Goerz, G. (1979). Günter Stüttgen zum 60. Geburtstag. [Günter Stüttgen on his 60th birthday]. Zeitschrift fur Hautkrankheiten, 54(2), 39-41.
Goerz, G. "Günter Stüttgen zum 60. Geburtstag." [Günter Stüttgen on his 60th birthday]. Zeitschrift fur Hautkrankheiten vol. 54,2 (1979): 39-41.
Goerz G. Günter Stüttgen zum 60. Geburtstag. [Günter Stüttgen on his 60th birthday]. Z Hautkr. 1979 Jan 15;54(2):39-41. German. PMID: 366938.
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[Wilhelm Schneider at 70].

Zeitschrift fur Hautkrankheiten

Adam W.
PMID: 6998155
Z Hautkr. 1980 Jun 01;55(11):697-701.

No abstract available.

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Adam W. Wilhelm Schneider zum 70. Geburstag. [Wilhelm Schneider at 70]. Z Hautkr. 1980;55(11):697-701
Adam, W. (1980). Wilhelm Schneider zum 70. Geburstag. [Wilhelm Schneider at 70]. Zeitschrift fur Hautkrankheiten, 55(11), 697-701.
Adam, W. "Wilhelm Schneider zum 70. Geburstag." [Wilhelm Schneider at 70]. Zeitschrift fur Hautkrankheiten vol. 55,11 (1980): 697-701.
Adam W. Wilhelm Schneider zum 70. Geburstag. [Wilhelm Schneider at 70]. Z Hautkr. 1980 Jun 01;55(11):697-701. German. PMID: 6998155.
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High-resolution structures of single-metal-substituted concanavalin A: the Co,Ca-protein at 1.6 A and the Ni,Ca-protein at 2.0 A.

Acta crystallographica. Section D, Biological crystallography

Emmerich C, Helliwell JR, Redshaw M, Naismith JH, Harrop SJ, Raftery J, Kalb AJ, Yariv J, Dauter Z, Wilson KS.
PMID: 15299372
Acta Crystallogr D Biol Crystallogr. 1994 Sep 01;50:749-56. doi: 10.1107/S0907444994002143.

The molecular structures of cobalt- and nickel-substituted concanavalin A have been refined at 1.6 and 2.0 A resolution, respectively. Both metal derivatives crystallize in space group I222 with approximate cell dimensions a = 89, b = 87 and c...

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Emmerich C, Helliwell JR, Redshaw M, et al. High-resolution structures of single-metal-substituted concanavalin A: the Co,Ca-protein at 1.6 A and the Ni,Ca-protein at 2.0 A. Acta Crystallogr D Biol Crystallogr. 1994;50:749-56doi: 10.1107/S0907444994002143.
Emmerich, C., Helliwell, J. R., Redshaw, M., Naismith, J. H., Harrop, S. J., Raftery, J., Kalb, A. J., Yariv, J., Dauter, Z., & Wilson, K. S. (1994). High-resolution structures of single-metal-substituted concanavalin A: the Co,Ca-protein at 1.6 A and the Ni,Ca-protein at 2.0 A. Acta crystallographica. Section D, Biological crystallography, 50749-56. https://doi.org/10.1107/S0907444994002143
Emmerich, C, et al. "High-resolution structures of single-metal-substituted concanavalin A: the Co,Ca-protein at 1.6 A and the Ni,Ca-protein at 2.0 A." Acta crystallographica. Section D, Biological crystallography vol. 50 (1994): 749-56. doi: https://doi.org/10.1107/S0907444994002143
Emmerich C, Helliwell JR, Redshaw M, Naismith JH, Harrop SJ, Raftery J, Kalb AJ, Yariv J, Dauter Z, Wilson KS. High-resolution structures of single-metal-substituted concanavalin A: the Co,Ca-protein at 1.6 A and the Ni,Ca-protein at 2.0 A. Acta Crystallogr D Biol Crystallogr. 1994 Sep 01;50:749-56. doi: 10.1107/S0907444994002143. PMID: 15299372.
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Showing 25 to 33 of 33 entries