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Crystallisation and preliminary X‐ray data of ribulose‐1,5‐bisphosphate carboxylase from spinach
Author(s) -
Barcena J.A.,
Pickersgill R.W.,
Adams M.J.,
Phillips D.C.,
Whatley F.R.
Publication year - 1983
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1002/j.1460-2075.1983.tb01747.x
Subject(s) - biology , spinach , rubisco , ribulose 1,5 bisphosphate , pyruvate carboxylase , biochemistry , photosynthesis , enzyme
Crystals of a tertiary complex of spinach ribulose‐1,5‐bisphosphate carboxylase/oxygenase with the activators Mg 2+ and CO 2 have been grown. These crystals diffract strongly to 1.6 Å resolution. The spacegroup is C222 1 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, L 8 S 8 ) 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 L 8 S 8 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.