Crystallization and preliminary neutron diffraction studies of HIV-1 protease cocrystallized with inhibitor KNI-272.
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.
Matsumura
Hiroyoshi
H
Graduate School of Engineering, Osaka University, Suita, Osaka 565-0871, Japan.
Adachi
Motoyasu
M
Sugiyama
Shigeru
S
Okada
Shino
S
Yamakami
Megumi
M
Tamada
Taro
T
Hidaka
Koushi
K
Hayashi
Yoshio
Y
Kimura
Tooru
T
Kiso
Yoshiaki
Y
Kitatani
Tomoya
T
Maki
Sho
S
Yoshikawa
Hiroshi Y
HY
Adachi
Hiroaki
H
Takano
Kazufumi
K
Murakami
Satoshi
S
Inoue
Tsuyoshi
T
Kuroki
Ryota
R
Mori
Yusuke
Y
D000595:Amino Acid Sequence; D003460:Crystallization / Q000379:methods*; D018360:Crystallography, X-Ray; D016333:HIV Protease / Q000737:chemistry*; D017320:HIV Protease Inhibitors / Q000737:chemistry*; D006801:Humans; D008969:Molecular Sequence Data; D033363:Neutron Diffraction; D009842:Oligopeptides / Q000737:chemistry*
D017320:HIV Protease Inhibitors; D009842:Oligopeptides; D016333:HIV Protease; C514803:p16 protease, Human immunodeficiency virus 1; C077822:kynostatin 272