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Crystallization of 5-aminolaevulinic acid dehydratase from Escherichia coli and Saccharomyces cerevisiae and preliminary X-ray characterization of the crystals

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Crystallization of 5-aminolaevulinic acid dehydratase from Escherichia coli and Saccharomyces cerevisiae and preliminary X-ray characterization of the crystals. / Erskine, P.T.; Cooper, J.; Lambert, R.; Lewis, G.; Wood, S.P.; Shoolingin-jordan, P.M.; Maignan, S.; Spencer, P.; Senior, N.; Awan, S.; Warren, M.; Tickle, I.J.; Thomas, P.

In: Protein Science, Vol. 6, No. 8, 01.08.1997, p. 1774-1776.

Research output: Contribution to journalArticlepeer-review

Harvard

Erskine, PT, Cooper, J, Lambert, R, Lewis, G, Wood, SP, Shoolingin-jordan, PM, Maignan, S, Spencer, P, Senior, N, Awan, S, Warren, M, Tickle, IJ & Thomas, P 1997, 'Crystallization of 5-aminolaevulinic acid dehydratase from Escherichia coli and Saccharomyces cerevisiae and preliminary X-ray characterization of the crystals', Protein Science, vol. 6, no. 8, pp. 1774-1776. https://doi.org/10.1002/pro.5560060820

APA

Erskine, P. T., Cooper, J., Lambert, R., Lewis, G., Wood, S. P., Shoolingin-jordan, P. M., Maignan, S., Spencer, P., Senior, N., Awan, S., Warren, M., Tickle, I. J., & Thomas, P. (1997). Crystallization of 5-aminolaevulinic acid dehydratase from Escherichia coli and Saccharomyces cerevisiae and preliminary X-ray characterization of the crystals. Protein Science, 6(8), 1774-1776. https://doi.org/10.1002/pro.5560060820

Vancouver

Author

Erskine, P.T. ; Cooper, J. ; Lambert, R. ; Lewis, G. ; Wood, S.P. ; Shoolingin-jordan, P.M. ; Maignan, S. ; Spencer, P. ; Senior, N. ; Awan, S. ; Warren, M. ; Tickle, I.J. ; Thomas, P. / Crystallization of 5-aminolaevulinic acid dehydratase from Escherichia coli and Saccharomyces cerevisiae and preliminary X-ray characterization of the crystals. In: Protein Science. 1997 ; Vol. 6, No. 8. pp. 1774-1776.

Bibtex

@article{b44de16726c54065b6c2c7c432e1fed3,
title = "Crystallization of 5-aminolaevulinic acid dehydratase from Escherichia coli and Saccharomyces cerevisiae and preliminary X-ray characterization of the crystals",
abstract = "5-Aminolaevulinic acid dehydratase (ALAD) catalyzes the formation of porphobilinogen from two molecules of 5-aminolaevulinic acid. Both Escherichia coli and Saccharomyces cerevisiae ALADs are homo-octameric enzymes which depend on Zn2+ for catalytic activity and are potently inhibited by lead ions. The E. coli enzyme crystallized in space group I422 (unit cell dimensions a = b = 130.7 A, c = 142.4 A). The best crystals were obtained in the presence of the covalently bound inhibitor laevulinic acid. The yeast enzyme (expressed in E. coli) crystallized in the same space group (I422) but with a smaller unit cell volume (a = b = 103.7 A, c = 167.7 A). High resolution synchrotron data sets were obtained from both E. coli and yeast ALAD crystals by cryocooling to 100 K.",
author = "P.T. Erskine and J. Cooper and R. Lambert and G. Lewis and S.P. Wood and P.M. Shoolingin-jordan and S. Maignan and P. Spencer and N. Senior and S. Awan and M. Warren and I.J. Tickle and P. Thomas",
year = "1997",
month = aug,
day = "1",
doi = "10.1002/pro.5560060820",
language = "English",
volume = "6",
pages = "1774--1776",
journal = "Protein Science",
issn = "0961-8368",
publisher = "Cold Spring Harbor Laboratory Press",
number = "8",

}

RIS

TY - JOUR

T1 - Crystallization of 5-aminolaevulinic acid dehydratase from Escherichia coli and Saccharomyces cerevisiae and preliminary X-ray characterization of the crystals

AU - Erskine, P.T.

AU - Cooper, J.

AU - Lambert, R.

AU - Lewis, G.

AU - Wood, S.P.

AU - Shoolingin-jordan, P.M.

AU - Maignan, S.

AU - Spencer, P.

AU - Senior, N.

AU - Awan, S.

AU - Warren, M.

AU - Tickle, I.J.

AU - Thomas, P.

PY - 1997/8/1

Y1 - 1997/8/1

N2 - 5-Aminolaevulinic acid dehydratase (ALAD) catalyzes the formation of porphobilinogen from two molecules of 5-aminolaevulinic acid. Both Escherichia coli and Saccharomyces cerevisiae ALADs are homo-octameric enzymes which depend on Zn2+ for catalytic activity and are potently inhibited by lead ions. The E. coli enzyme crystallized in space group I422 (unit cell dimensions a = b = 130.7 A, c = 142.4 A). The best crystals were obtained in the presence of the covalently bound inhibitor laevulinic acid. The yeast enzyme (expressed in E. coli) crystallized in the same space group (I422) but with a smaller unit cell volume (a = b = 103.7 A, c = 167.7 A). High resolution synchrotron data sets were obtained from both E. coli and yeast ALAD crystals by cryocooling to 100 K.

AB - 5-Aminolaevulinic acid dehydratase (ALAD) catalyzes the formation of porphobilinogen from two molecules of 5-aminolaevulinic acid. Both Escherichia coli and Saccharomyces cerevisiae ALADs are homo-octameric enzymes which depend on Zn2+ for catalytic activity and are potently inhibited by lead ions. The E. coli enzyme crystallized in space group I422 (unit cell dimensions a = b = 130.7 A, c = 142.4 A). The best crystals were obtained in the presence of the covalently bound inhibitor laevulinic acid. The yeast enzyme (expressed in E. coli) crystallized in the same space group (I422) but with a smaller unit cell volume (a = b = 103.7 A, c = 167.7 A). High resolution synchrotron data sets were obtained from both E. coli and yeast ALAD crystals by cryocooling to 100 K.

U2 - 10.1002/pro.5560060820

DO - 10.1002/pro.5560060820

M3 - Article

VL - 6

SP - 1774

EP - 1776

JO - Protein Science

JF - Protein Science

SN - 0961-8368

IS - 8

ER -

ID: 4000497