• Something wrong with this record ?

Crystallization and diffraction analysis of β-N-acetylhexosaminidase from Aspergillus oryzae

O. Vaněk, J. Brynda, K. Hofbauerová, Z. Kukačka, P. Pachl, K. Bezouška, P. Rezáčová,

. 2011 ; 67 (Pt 4) : 498-503. [pub] 20110326

Language English Country England, Great Britain

Document type Journal Article, Research Support, Non-U.S. Gov't, Research Support, U.S. Gov't, Non-P.H.S.

Persistent link   https://www.medvik.cz/link/bmc12027611

Fungal β-N-acetylhexosaminidases are enzymes that are used in the chemoenzymatic synthesis of biologically interesting oligosaccharides. The enzyme from Aspergillus oryzae was produced and purified from its natural source and crystallized using the hanging-drop vapour-diffusion method. Diffraction data from two crystal forms (primitive monoclinic and primitive tetragonal) were collected to resolutions of 3.2 and 2.4 Å, respectively. Electrophoretic and quantitative N-terminal protein-sequencing analyses confirmed that the crystals are formed by a complete biologically active enzyme consisting of a glycosylated catalytic unit and a noncovalently attached propeptide.

References provided by Crossref.org

000      
00000naa a2200000 a 4500
001      
bmc12027611
003      
CZ-PrNML
005      
20121206103236.0
007      
ta
008      
120817e20110326enk f 000 0#eng||
009      
AR
024    7_
$a 10.1107/s1744309111004945 $2 doi
035    __
$a (PubMed)21505251
040    __
$a ABA008 $b cze $d ABA008 $e AACR2
041    0_
$a eng
044    __
$a enk
100    1_
$a Vaněk, Ondřej $u Institute of Microbiology, Academy of Sciences of the Czech Republic, Vídeňská 1083, 14220 Prague, Czech Republic.
245    10
$a Crystallization and diffraction analysis of β-N-acetylhexosaminidase from Aspergillus oryzae / $c O. Vaněk, J. Brynda, K. Hofbauerová, Z. Kukačka, P. Pachl, K. Bezouška, P. Rezáčová,
520    9_
$a Fungal β-N-acetylhexosaminidases are enzymes that are used in the chemoenzymatic synthesis of biologically interesting oligosaccharides. The enzyme from Aspergillus oryzae was produced and purified from its natural source and crystallized using the hanging-drop vapour-diffusion method. Diffraction data from two crystal forms (primitive monoclinic and primitive tetragonal) were collected to resolutions of 3.2 and 2.4 Å, respectively. Electrophoretic and quantitative N-terminal protein-sequencing analyses confirmed that the crystals are formed by a complete biologically active enzyme consisting of a glycosylated catalytic unit and a noncovalently attached propeptide.
650    _2
$a Aspergillus oryzae $x enzymologie $7 D001236
650    _2
$a katalytická doména $7 D020134
650    _2
$a krystalizace $7 D003460
650    _2
$a krystalografie rentgenová $7 D018360
650    _2
$a glykosylace $7 D006031
650    _2
$a beta-N-acetylhexosaminidasy $x chemie $x metabolismus $7 D001619
655    _2
$a časopisecké články $7 D016428
655    _2
$a práce podpořená grantem $7 D013485
655    _2
$a Research Support, U.S. Gov't, Non-P.H.S. $7 D013486
700    1_
$a Brynda, Jiří
700    1_
$a Hofbauerová, Kateřina
700    1_
$a Kukačka, Zdeněk
700    1_
$a Pachl, Petr
700    1_
$a Bezouška, Karel
700    1_
$a Rezáčová, Pavlína
773    0_
$w MED00179506 $t Acta crystallographica. Section F, Structural biology and crystallization communications $x 1744-3091 $g Roč. 67, č. Pt 4 (20110326), s. 498-503
856    41
$u https://pubmed.ncbi.nlm.nih.gov/21505251 $y Pubmed
910    __
$a ABA008 $b sig $c sign $y m
990    __
$a 20120817 $b ABA008
991    __
$a 20121206103309 $b ABA008
999    __
$a ok $b bmc $g 949653 $s 784957
BAS    __
$a 3
BAS    __
$a PreBMC
BMC    __
$a 2011 $b 67 $c Pt 4 $d 498-503 $e 20110326 $i 1744-3091 $m Acta crystallographica. Section F $n Acta Crystallogr Sect F Struct Biol Cryst Commun $x MED00179506
LZP    __
$a Pubmed-20120817/11/03

Find record

Citation metrics

Archiving options