Structure of Complex of Synthetic HIV-1 Protease with a Substrate-Based Inhibitor at 2.3 Å Resolution-Reference-Cited by-同舟云学术

Structure of Complex of Synthetic HIV-1 Protease with a Substrate-Based Inhibitor at 2.3 Å Resolution

Published:1989-12 Issue:4934 Volume:246 Page:1149-1152
ISSN:0036-8075
Container-title:Science
language:en
Short-container-title:Science

Author:

Miller Maria¹,Schneider Jens²,Sathyanarayana Bangalore K.¹,Toth Mihaly V.³,Marshall Garland R.³,Clawson Leigh²,Selk Linda²,Kent Stephen B. H.²,Wlodawer Alexander¹

Affiliation:

1. Crystalography Laboratory, NCI-Frederick Cancer Research Facility, BRI-Basic Research Program, MD 21701.

2. Division of Biology, California Institute of Technology, Pasadena, CA 91125.

3. Department of Pharmacology, Washington University School of Medicine, St. Louis, MO 63110.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

Reference20 articles.

1. Crystallographic R Factor Refinement by Molecular Dynamics

2. FEHRENTZ, J.A., SYNTHESIS-STUTTGART 8: 676 (1983).

3. FITZGERALD, P. M. D., JOURNAL OF APPLIED CRYSTALLOGRAPHY 21: 273 (1988).

4. HENDRICKSON, W.A., STEREOCHEMICALLY RESTRAINED REFINEMENT OF MACROMOLECULAR STRUCTURES, METHODS IN ENZYMOLOGY 115: 252 (1985).

5. HOWARD, A.J., THE USE OF AN IMAGING PROPORTIONAL COUNTER IN MACROMOLECULAR CRYSTALLOGRAPHY, JOURNAL OF APPLIED CRYSTALLOGRAPHY 20: 383 (1987).

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