Purification, co-crystallization and preliminary X-ray analysis of the natural aspartic proteinase inhibitor I(A)3 complexed with saccharopepsin from Saccharomyces cerevisiae
Purification, co-crystallization and preliminary X-ray analysis of the natural aspartic proteinase inhibitor I(A)3 complexed with saccharopepsin from Saccharomyces cerevisiae
The vacuolar aspartic proteinase from baker's yeast, saccharopepsin, has been co-crystallized with its natural inhibitor IA3, found in the cytosol. The IA3-saccharopepsin complex crystals belong to the space group P6222, with unit-cell parameters a = b = 192.1, c = 59.80 Å and one molecule per asymmetric unit. The initial X-ray analysis of the complex indicates that the crystals diffract to 5.0 Å, similar to native saccharopepsin crystals. This is probably a consequence in part of glycosylation of the native saccharopepsin. Full structural analysis of the complex crystal is in progress.
aspartic proteinases, inhibitors, saccharopepsin
915-917
Badasso, M.O.
59a5d949-d29d-4be7-ab09-930dcf76d889
Read, J.A.
7abaa518-cbdb-46f7-858c-ad45a35ae082
Dhanaraj, V.
60666c14-e81e-47cf-ba59-a18d5d98ccd8
Cooper, J.B.
d9f0f6a8-1260-48fc-aa5c-3dbc650e3ec0
Wood, S.P.
430faabf-7f5c-4cf6-9bcc-5955f5e09566
Blundell, T.L.
7311fa34-6cbd-45da-ba4e-cfdafe447180
Dreyer, T.
c109e4f3-fff1-4c3f-86ac-d84a7a500541
Winther, J.
413083f8-d9f5-4421-9164-cdd671962ecc
1 July 2000
Badasso, M.O.
59a5d949-d29d-4be7-ab09-930dcf76d889
Read, J.A.
7abaa518-cbdb-46f7-858c-ad45a35ae082
Dhanaraj, V.
60666c14-e81e-47cf-ba59-a18d5d98ccd8
Cooper, J.B.
d9f0f6a8-1260-48fc-aa5c-3dbc650e3ec0
Wood, S.P.
430faabf-7f5c-4cf6-9bcc-5955f5e09566
Blundell, T.L.
7311fa34-6cbd-45da-ba4e-cfdafe447180
Dreyer, T.
c109e4f3-fff1-4c3f-86ac-d84a7a500541
Winther, J.
413083f8-d9f5-4421-9164-cdd671962ecc
Badasso, M.O., Read, J.A., Dhanaraj, V., Cooper, J.B., Wood, S.P., Blundell, T.L., Dreyer, T. and Winther, J.
(2000)
Purification, co-crystallization and preliminary X-ray analysis of the natural aspartic proteinase inhibitor I(A)3 complexed with saccharopepsin from Saccharomyces cerevisiae.
Acta Crystallographica Section D: Biological Crystallography, 56 (7), .
(doi:10.1107/S090744490000737X).
Abstract
The vacuolar aspartic proteinase from baker's yeast, saccharopepsin, has been co-crystallized with its natural inhibitor IA3, found in the cytosol. The IA3-saccharopepsin complex crystals belong to the space group P6222, with unit-cell parameters a = b = 192.1, c = 59.80 Å and one molecule per asymmetric unit. The initial X-ray analysis of the complex indicates that the crystals diffract to 5.0 Å, similar to native saccharopepsin crystals. This is probably a consequence in part of glycosylation of the native saccharopepsin. Full structural analysis of the complex crystal is in progress.
Full text not available from this repository.
More information
Published date: 1 July 2000
Keywords:
aspartic proteinases, inhibitors, saccharopepsin
Identifiers
Local EPrints ID: 56570
URI: https://eprints.soton.ac.uk/id/eprint/56570
ISSN: 0907-4449
PURE UUID: ea4c151b-34b7-461b-a75a-844016f06aa0
Catalogue record
Date deposited: 06 Aug 2008
Last modified: 13 Mar 2019 20:35
Export record
Altmetrics
Contributors
Author:
M.O. Badasso
Author:
J.A. Read
Author:
V. Dhanaraj
Author:
J.B. Cooper
Author:
S.P. Wood
Author:
T.L. Blundell
Author:
T. Dreyer
Author:
J. Winther
University divisions
Download statistics
Downloads from ePrints over the past year. Other digital versions may also be available to download e.g. from the publisher's website.
View more statistics