Abstract
Human ketohexokinase has been produced in E. coli, purified and crystallized in an orthorhombic form (space group P21212 or P212121) with four protein molecules in the asymmetric unit.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 586-588 |
| Number of pages | 3 |
| Journal | Acta Crystallographica Section D: Biological Crystallography |
| Volume | 57 |
| Issue number | 4 |
| DOIs | |
| State | Published - 2001 |
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ASJC Scopus subject areas
- Clinical Biochemistry
- Biochemistry, Genetics and Molecular Biology(all)
- Biochemistry
- Biophysics
- Condensed Matter Physics
- Structural Biology
Cite this
Expression, purification and preliminary crystallographic studies of human ketohexokinase. / Kozak, M.; Hayward, B.; Borek, D.; Bonthron, D. T.; Jaskólski, M.
In: Acta Crystallographica Section D: Biological Crystallography, Vol. 57, No. 4, 2001, p. 586-588.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Expression, purification and preliminary crystallographic studies of human ketohexokinase
AU - Kozak, M.
AU - Hayward, B.
AU - Borek, D.
AU - Bonthron, D. T.
AU - Jaskólski, M.
PY - 2001
Y1 - 2001
N2 - Human ketohexokinase has been produced in E. coli, purified and crystallized in an orthorhombic form (space group P21212 or P212121) with four protein molecules in the asymmetric unit.
AB - Human ketohexokinase has been produced in E. coli, purified and crystallized in an orthorhombic form (space group P21212 or P212121) with four protein molecules in the asymmetric unit.
UR - http://www.scopus.com/inward/record.url?scp=0035068461&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0035068461&partnerID=8YFLogxK
U2 - 10.1107/S0907444901001007
DO - 10.1107/S0907444901001007
M3 - Article
C2 - 11264590
AN - SCOPUS:0035068461
VL - 57
SP - 586
EP - 588
JO - Acta Crystallographica Section D: Structural Biology
JF - Acta Crystallographica Section D: Structural Biology
SN - 0907-4449
IS - 4
ER -