Crystallization, preliminary X-ray diffraction and structure analysis of Thermotoga maritima mannitol dehydrogenase

Journal Article · Sun Apr 01 00:00:00 EDT 2007 · Acta Crystallographica. Section F

DOI:https://doi.org/10.1107/S1744309107013097· OSTI ID:22360315

Puttick, Jennifer ^[1]; Vieille, Claire; Song, Seung H. ^[2]; Fodje, Michel N.; Grochulski, Pawel ^[3]; Delbaere, Louis T. J., ^[1]

---

1. Department of Biochemistry, University of Saskatchewan, Saskatoon, Saskatchewan S7N 5E5 (Canada)
2. Department of Biochemistry and Molecular Biology, Michigan State University, East Lansing, MI 48824-1319 (United States)
3. Canadian Macromolecular Facility, Canadian Light Source Inc., University of Saskatchewan, Saskatoon, Saskatchewan S7N 0X4 (Canada)

T. maritima mannitol dehydrogenase has been crystallized in space group P2{sub 1}2{sub 1}2{sub 1} with a = 84.43, b = 120.61, c = 145.76 Å. The crystals diffracted to 3.3 Å resolution at the Canadian Light Source. Diffraction data have been collected from a crystal of Thermotoga maritima mannitol dehydrogenase at the Canadian Light Source. The crystal diffracted to 3.3 Å resolution and belongs to space group P2{sub 1}2{sub 1}2{sub 1}, with unit-cell parameters a = 83.43, b = 120.61, c = 145.76 Å. The structure is likely to be solved by molecular replacement.

• OSTI ID: 22360315
• Journal Information: Acta Crystallographica. Section F, Journal Name: Acta Crystallographica. Section F Journal Issue: Pt 4 Vol. 63; ISSN ACSFCL; ISSN 1744-3091
• Country of Publication: United Kingdom
• Language: English

Related Subjects

75 CONDENSED MATTER PHYSICS
SUPERCONDUCTIVITY AND SUPERFLUIDITY
CRYSTALLIZATION
CRYSTALS
LIGHT SOURCES
RESOLUTION
SPACE GROUPS
X-RAY DIFFRACTION