| Literature DB >> 18997326 |
Hiroyoshi Matsumura1, Motoyasu Adachi, Shigeru Sugiyama, Shino Okada, Megumi Yamakami, Taro Tamada, Koushi Hidaka, Yoshio Hayashi, Tooru Kimura, Yoshiaki Kiso, Tomoya Kitatani, Sho Maki, Hiroshi Y Yoshikawa, Hiroaki Adachi, Kazufumi Takano, Satoshi Murakami, Tsuyoshi Inoue, Ryota Kuroki, Yusuke Mori.
Abstract
This paper reports the crystallization and preliminary neutron diffraction measurements of HIV-1 protease, a potential target for anti-HIV therapy, complexed with an inhibitor (KNI-272). The aim of this neutron diffraction study is to obtain structural information about the H atoms and to determine the protonation states of the residues within the active site. The crystal was grown to a size of 1.4 mm(3) by repeated macroseeding and a slow-cooling method using a two-liquid system. Neutron diffraction data were collected at room temperature using a BIX-4 diffractometer at the JRR-3 research reactor of the Japan Atomic Energy Agency (JAEA). The data set was integrated and scaled to 2.3 A resolution in space group P2(1)2(1)2, with unit-cell parameters a = 59.5, b = 87.4, c = 46.8 A.Entities:
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Year: 2008 PMID： 18997326 PMCID： PMC2581681 DOI： 10.1107/S1744309108029679
Source DB: PubMed Journal: Acta Crystallogr Sect F Struct Biol Cryst Commun ISSN： 1744-3091