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Title
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Crystals of HIV-1 reverse transcriptase diffracting to 2.2 A resolution.
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Authors
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D.K.Stammers,
D.O.Somers,
C.K.Ross,
I.Kirby,
P.H.Ray,
J.E.Wilson,
M.Norman,
J.S.Ren,
R.M.Esnouf,
E.F.Garman.
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Ref.
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J Mol Biol, 1994,
242,
586-588.
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PubMed id
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Abstract
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Reverse transcriptase (RT) from the human immunodeficiency virus type 1 has been
crystallized in four closely related forms, the best of which diffract X-rays to
2.2 A resolution. The RT was crystallized as a complex with a non-nucleoside
inhibitor, either nevirapine or a nevirapine analogue. Crystals grew from 6% PEG
3400 buffered at pH 5. These were of space group P2(1)2(1)2(1) with unit cell
parameters a = 147 A, b = 112 A, c = 79 A (form A), with one RT heterodimer in
the asymmetric unit. Changes in unit cell parameters and degree of crystalline
order were observed on soaking pregrown crystals in various solutions, giving
three further sets of unit cells. These were a = 143 A, b = 112, A, c = 79 A
(form B), a = 141 A, b = 111 A, c = 73 A (form C), a = 143 A, b = 117 A, c =
66.5 A (form D). The last two forms diffract X-rays to 2.2 A resolution.
Structure determinations of these latter crystal forms of RT should give a
detailed atomic model for this therapeutically important drug target.
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