| Title : Characterization of crystals of Penicillium purpurogenum acetyl xylan esterase from high-resolution x-ray diffraction - Pangborn_1996_Proteins_24_523 |
| Author(s) : Pangborn W , Erman M , Li N , Burkhart BM , Pletnev VZ , Duax WL , Gutierrez R , Peirano A , Eyzaguirre J , Thiel DJ , Ghosh D |
| Ref : Proteins , 24 :523 , 1996 |
|
Abstract :
Acetyl xylan esterase from Penicillium purpurogenum, a single-chain 23 kDa member of a newly characterized family of esterases that cleaves side chain ester linkages in xylan, has been crystallized. The crystals diffract to better than 1 A resolution at the Cornell High Energy Synchrotron Source (CHESS) and are highly stable in the synchrotron radiation. The space group is P2(1)2(1)2(1) and cell dimensions are a = 34.9 A, b = 61.0 A, C = 72.5 A. |
| PubMedSearch : Pangborn_1996_Proteins_24_523 |
| PubMedID: 8860002 |
Pangborn W, Erman M, Li N, Burkhart BM, Pletnev VZ, Duax WL, Gutierrez R, Peirano A, Eyzaguirre J, Thiel DJ, Ghosh D (1996)
Characterization of crystals of Penicillium purpurogenum acetyl xylan esterase from high-resolution x-ray diffraction
Proteins
24 :523
Pangborn W, Erman M, Li N, Burkhart BM, Pletnev VZ, Duax WL, Gutierrez R, Peirano A, Eyzaguirre J, Thiel DJ, Ghosh D (1996)
Proteins
24 :523