Open AccessCrystallization and preliminary neutron diffraction studies of HIV‐1 protease cocrystallized with inhibitor KNI‐272
Author(s) -
Matsumura Hiroyoshi,
Adachi Motoyasu,
Sugiyama Shigeru,
Okada Shino,
Yamakami Megumi,
Tamada Taro,
Hidaka Koushi,
Hayashi Yoshio,
Kimura Tooru,
Kiso Yoshiaki,
Kitatani Tomoya,
Maki Sho,
Yoshikawa Hiroshi Y.,
Adachi Hiroaki,
Takano Kazufumi,
Murakami Satoshi,
Inoue Tsuyoshi,
Kuroki Ryota,
Mori Yusuke
Publication year - 2008
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309108029679
Subject(s) - neutron diffraction , crystallography , crystallization , materials science , diffraction , diffractometer , resolution (logic) , protonation , crystal structure , chemistry , physics , organic chemistry , optics , artificial intelligence , computer science , ion
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 Å resolution in space group P 2 1 2 1 2, with unit‐cell parameters a = 59.5, b = 87.4, c = 46.8 Å.