Detailed Information on Publication Record
2001
Purification, Crystallization and Preliminary X-ray Analysis of a Maize Cytokinin-glucoside-specific b-Glucosidase.
VÉVODOVÁ, Jitka, Jaromír MAREK, Jan ZOUHAR, Břetislav BRZOBOHATÝ, X.-D. SU et. al.Basic information
Original name
Purification, Crystallization and Preliminary X-ray Analysis of a Maize Cytokinin-glucoside-specific b-Glucosidase.
Authors
VÉVODOVÁ, Jitka, Jaromír MAREK, Jan ZOUHAR, Břetislav BRZOBOHATÝ and X.-D. SU
Edition
Acta Crystallogr., Sect.D, Dánsko, 2001, 0907-4449
Other information
Language
English
Type of outcome
Článek v odborném periodiku
Field of Study
10600 1.6 Biological sciences
Country of publisher
Denmark
Confidentiality degree
není předmětem státního či obchodního tajemství
Impact factor
Impact factor: 2.124
RIV identification code
RIV/00216224:14310/01:00002609
Organization unit
Faculty of Science
Keywords in English
beta-glucosidase; hydrolase; protein crystallography
Změněno: 7/12/2001 15:52, prof. RNDr. Břetislav Brzobohatý, CSc.
Abstract
V originále
Zm-p60.1, a cytokinin-glucoside-specific beta-glucosidase from maize, is a key enzyme involved in plant development and growth. It has been over-expressed in soluble form from Escherichia coli with a His tag at its N-terminus. The recombinant protein has been purified and crystallized at room temperature using PEG 4000 as main precipitant. A few forms of crystals have been observed from very similar conditions. A flash-annealed monoclinic crystal diffracted to high resolution (beyond 2 A) with space group P21, and unit-cell parameters a = 55.66 A, b = 110.72 A, c = 72.94 A, b = 92.10 deg. The asymmetric unit is estimated and confirmed by molecular replacement solution to contain a Zm-p60.1 dimer, giving a crystal volume per protein mass (Vm) of 1.89 A3 Da-1 and a solvent content of 35%.
Links
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