M O Badasso
Overview
Explore the profile of M O Badasso including associated specialties, affiliations and a list of published articles.
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8
Citations
337
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Recent Articles
1.
Simpson A, Leiman P, Tao Y, He Y, Badasso M, Jardine P, et al.
Acta Crystallogr D Biol Crystallogr
. 2001 Aug;
57(Pt 9):1260-9.
PMID: 11526317
The head-tail connector of bacteriophage phi29 is composed of 12 36 kDa subunits with 12-fold symmetry. It is the central component of a rotary motor that packages the genomic dsDNA...
2.
Simpson A, Tao Y, Leiman P, Badasso M, He Y, Jardine P, et al.
Nature
. 2000 Dec;
408(6813):745-50.
PMID: 11130079
Motors generating mechanical force, powered by the hydrolysis of ATP, translocate double-stranded DNA into preformed capsids (proheads) of bacterial viruses and certain animal viruses. Here we describe the motor that...
3.
Cronin N, Badasso M, Tickle I, Dreyer T, Hoover D, Rosati R, et al.
J Mol Biol
. 2000 Nov;
303(5):745-60.
PMID: 11061973
Saccharopepsin is a vacuolar aspartic proteinase involved in activation of a number of hydrolases. The enzyme has great structural homology to mammalian aspartic proteinases including human renin and we have...
4.
Badasso M, Leiman P, Tao Y, He Y, Ohlendorf D, Rossmann M, et al.
Acta Crystallogr D Biol Crystallogr
. 2000 Aug;
56(Pt 9):1187-90.
PMID: 10957642
The head-tail connector of bacteriophage phi29, an oligomer of gene product 10 (gp10), was crystallized into various forms. The most useful of these were an orthorhombic P22(1)2(1) form (unit-cell parameters...
5.
Badasso M, Read J, Dhanaraj V, Cooper J, Wood S, Blundell T, et al.
Acta Crystallogr D Biol Crystallogr
. 2000 Aug;
56(Pt 7):915-7.
PMID: 10930843
The vacuolar aspartic proteinase from baker's yeast, saccharopepsin, has been co-crystallized with its natural inhibitor I(A)3, found in the cytosol. The I(A)3-saccharopepsin complex crystals belong to the space group P6(2)22,...
6.
Bunting K, Cooper J, Badasso M, Tickle I, Newton M, Wood S, et al.
Eur J Biochem
. 1998 Mar;
251(3):795-803.
PMID: 9490054
We have refined the X-ray structures of two site-directed mutants of the iron-dependent superoxide dismutase (SOD) from Mycobacterium tuberculosis. These mutations which affect residue 145 in the enzyme (H145Q and...
7.
Cooper J, Saward S, Erskine P, Badasso M, Wood S, Zhang Y, et al.
FEBS Lett
. 1996 Jun;
387(2-3):105-8.
PMID: 8674528
We have refined the X-ray structure of a site-directed G152A mutant of the iron-dependent superoxide dismutase from Mycobacterium tuberculosis at 2.9 angstroms resolution. The mutation which replaces a glycine residue...
8.
Cooper J, McIntyre K, Badasso M, Wood S, Zhang Y, Garbe T, et al.
J Mol Biol
. 1995 Mar;
246(4):531-44.
PMID: 7877174
The X-ray structure of the tetrameric iron-dependent superoxide dismutase from Mycobacterium tuberculosis has been refined to an R-factor of 0.167 and a correlation coefficient of 0.954 at 2.0 A resolution....