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. 1983;2(12):2363–2367. doi: 10.1002/j.1460-2075.1983.tb01747.x

Crystallisation and preliminary X-ray data of ribulose-1,5-bisphosphate carboxylase from spinach

JA Barcena 1,2, RW Pickersgill 1, MJ Adams 1,*, DC Phillips 1, FR Whatley 1
PMCID: PMC555458  PMID: 16453489

Abstract

Crystals of a tertiary complex of spinach ribulose-1,5-bisphosphate carboxylase/oxygenase with the activators Mg2+ and CO2 have been grown. These crystals diffract strongly to 1.6 Å resolution. The spacegroup is C2221 with unit cell dimensions a = 158.6 Å, b = 158.6 Å, c = 203.4 Å. Additional local symmetry is apparent in the pattern of absences and the intensity distribution of the X-ray precession photographs. The photographs have been interpreted in terms of a molecule (consisting of eight large and eight small subunits, L8S8) with 222 symmetry and a molecular centre shifted 2 Å in the x direction from the origin of the unit cell. The asymmetric unit contains half the L8S8 molecule. The intensity distribution suggests that the molecular symmetry does not deviate far from 422. These crystals are compared with other crystalline forms of the enzyme and the implications of these results are discussed.

Keywords: carboxylase, crystallisation, purification, ribulosebis-phosphate, X-ray

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2364Fig. 1.
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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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