Crystallization and preliminary crystallographic analysis of human L-xylulose reductase.
Human L-xylulose reductase was crystallized from buffered polyethylene glycol solutions using the hanging-drop vapour-diffusion method. The crystals diffract to 2.1 A resolution and belong to the orthorhombic P222 space group, with unit-cell parameters a = 72.9, b = 74.1, c = 87.9 A. This is the first crystallization report of a xylulose reductase that is identical to diacetyl reductase.
Department of Medicinal Chemistry, Victorian College of Pharmacy, Monash University(Parkville Campus), Parkville, Victoria 3052, Australia. ossama.el-kabbani@vcp.monash.edu.au
Ossama
O
El-Kabbani
Roland P T
RP
Chung
Syuhei
S
Ishikura
Noriyuki
N
Usami
Junichi
J
Nakagawa
Akira
A
Hara
D003460:Crystallization; D018360:Crystallography, X-Ray; D006801:Humans; D015394:Molecular Structure; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification; D013401:Sugar Alcohol Dehydrogenases / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification
D011994:Recombinant Proteins; D013401:Sugar Alcohol Dehydrogenases; C023300:L-xylulose reductase