Acta Crystallographica Section D

Biological Crystallography

Volume 63, Part 4 (April 2007)



[Issue Author Index][Volume Author Index]
[Cover illustration] Cover illustration: 2Fo - Fc map for the CN- bound form of Arthromyces ramosus peroxidase at 1.3 Å resolution (contour level: green 2[sigma], red 6[sigma])(p. 472).

research papers


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Acta Cryst. (2007). D63, 431-436  [ doi:10.1107/S0907444907000546 ]

Structure of the transcription regulator CcpA from Lactococcus lactis

B. Loll, M. Kowalczyk, C. Alings, A. Chieduch, J. Bardowski, W. Saenger and J. Biesiadka

Synopsis: The crystal structure of L. lactis CcpA is reported.

PDB reference: 2o20

Online 16 March 2007


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Acta Cryst. (2007). D63, 437-446  [ doi:10.1107/S0907444907001631 ]

Carbohydrate-binding properties of goat secretory glycoprotein (SPG-40) and its functional implications: structures of the native glycoprotein and its four complexes with chitin-like oligosaccharides

J. Kumar, A. S. Ethayathulla, D. B. Srivastava, N. Singh, S. Sharma, P. Kaur, A. Srinivasan and T. P. Singh

Synopsis: The crystal structures of four complexes of a signalling glycoprotein from goat (SPG-40) with oligosaccharides of different lengths have been determined. The structures of the complexes with GlcNAc3, GlcNAc4, GlcNAc5 and GlcNAc6 revealed the positions of these oligosaccharides in the carbohydrate-binding groove and provided insights into the binding mechanism of oligosaccharides to SPG-40.

PDB references: 2dsz, 2dt0, 2dt1, 2dt2 and 2dt3

Online 16 March 2007


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Acta Cryst. (2007). D63, 447-457  [ doi:10.1107/S0907444907002661 ]

Automated search-model discovery and preparation for structure solution by molecular replacement

R. M. Keegan and M. D. Winn

Synopsis: An automation pipeline for macromolecular structure solution by molecular replacement with a special emphasis on the discovery and preparation of a large number of search models is described. It is concluded that exploring a range of search models automatically can be valuable in many cases.

Online 16 March 2007


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Acta Cryst. (2007). D63, 458-464  [ doi:10.1107/S0907444907003228 ]

Packing and loop-structure variations in non-isomorphous crystals of FabZ from Plasmodium falciparum

P. L. Swarnamukhi, S. K. Sharma, P. Padala, N. Surolia, A. Surolia and K. Suguna

Synopsis: The crystal structures of FabZ from P. falciparum in two crystal forms are reported and a detailed structural comparison is made of three crystal forms of this enzyme in order to explore the possible reasons for the existence of non-isomorphism.

PDB references: 2oki and 2okh

Online 16 March 2007


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Acta Cryst. (2007). D63, 465-471  [ doi:10.1107/S0907444907003320 ]

Structures of the dimerization domains of the Escherichia coli disulfide-bond isomerase enzymes DsbC and DsbG

S.-M. Yeh, N. Koon, C. Squire and P. Metcalf

Synopsis: The crystal structures of the separate dimerization domains of the periplasmic disulfide-bond isomerases DsbC and DsbG have been determined at resolutions of 2.0 and 1.9 Å, respectively.

PDB references: 2iyj and 2iy2

Online 16 March 2007


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Acta Cryst. (2007). D63, 472-477  [ doi:10.1107/S0907444907003812 ]

Structures of cyanide, nitric oxide and hydroxylamine complexes of Arthromyces ramosus peroxidase at 100 K refined to 1.3 Å resolution: coordination geometries of the ligands to the haem iron

K. Fukuyama and T. Okada

Synopsis: Crystal structures of CN--, NO- and hydroxylamine-bound forms of A. ramosus peroxidase at 1.3 Å resolution show the coordination geometries of the ligands to the haem iron.

PDB references: 2e39, 2e3a and 2e3b

Online 16 March 2007


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Acta Cryst. (2007). D63, 478-485  [ doi:10.1107/S0907444907005045 ]

Crystallographic analysis of Bacillus subtilis CsaA

Y. A. Shapova and M. Paetzel

Synopsis: The structure of the protein-targeting chaperone CsaA from B. subtilis has been solved to 2.0 Å resolution from a trigonal crystal form (P3221) and to 1.9 Å resolution from a tetragonal crystal form (P4212).

PDB references: 2nzo and 2nzh

Online 16 March 2007


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Acta Cryst. (2007). D63, 486-492  [ doi:10.1107/S0907444907005264 ]

Cryogenic (<20 K) helium cooling mitigates radiation damage to protein crystals

U. Chinte, B. Shah, Y.-S. Chen, A. A. Pinkerton, C. A. Schall and B. L. Hanson

Synopsis: Comparison of diffraction data collected from matched protein crystals bathed in helium at a set temperature of 8 K and nitrogen at 100 K indicate that the use of cryogenic helium can increase the diffractive lifetime of crystals and measurably mitigate radiation damage.

Online 16 March 2007


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Acta Cryst. (2007). D63, 493-499  [ doi:10.1107/S0907444907006592 ]

ADP-2Ho as a phasing tool for nucleotide-containing proteins

S.-Y. Ku, G. D. Smith and P. L. Howell

Synopsis: The application of ADP-2Ho as a heavy-atom derivative for the structure determination of MTR kinase is described.

PDB reference: 2olc

Online 16 March 2007


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Acta Cryst. (2007). D63, 500-507  [ doi:10.1107/S090744490700697X ]

Structure of the complex of trypsin with a highly potent synthetic inhibitor at 0.97 Å resolution

M. Sherawat, P. Kaur, M. Perbandt, C. Betzel, W. A. Slusarchyk, G. S. Bisacchi, C. Chang, B. L. Jacobson, H. M. Einspahr and T. P. Singh

Synopsis: The crystal structure of trypsin with a designed highly potent synthetic inhibitor has been determined at atomic resolution. The structure has revealed the precise nature of the interactions between the enzyme and the inhibitor molecules.

PDB reference: 2ayw

Online 16 March 2007


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Acta Cryst. (2007). D63, 508-513  [ doi:10.1107/S090744490700902X ]

Human glutamate carboxypeptidase II inhibition: structures of GCPII in complex with two potent inhibitors, quisqualate and 2-PMPA

J. R. Mesters, K. Henning and R. Hilgenfeld

Synopsis: Crystal structures were determined of the extracellular part of glutamate carboxypeptidase II (GCPII; amino-acid residues 44-750) in complex with two potent inhibitors, quisqualate and 2-PMPA (the most potent GCPII inhibitor to date), at resolutions of 3.0 and 2.2 Å, respectively.

PDB references: 2jbk and 2jbj

Online 16 March 2007


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Acta Cryst. (2007). D63, 514-525  [ doi:10.1107/S0907444907000844 ]

CAALIGN: a program for pairwise and multiple protein-structure alignment

T. J. Oldfield

Synopsis: The program CAALIGN performs pairwise structure alignment and multiple structure alignment of protein structures based on the maximal superposition of C[alpha] coordinates.

Online 16 March 2007


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Acta Cryst. (2007). D63, 526-535  [ doi:10.1107/S0907444906056137 ]

A method for the general identification of protein crystals in crystallization experiments using a noncovalent fluorescent dye

M. R. Groves, I. B. Müller, X. Kreplin and J. Müller-Dieckmann

Synopsis: A method is described whereby the addition of a nonspecific fluorescent dye to a wide variety of different protein solutions prior to crystallization results in a significantly increased fluorescence signal being obtained from protein crystals. Subsequent fluorescence imaging of the crystallization experiments demonstrates that successful experiments containing crystals may be easily discriminated from other objects produced by the crystallization experiment.

Online 16 March 2007


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Acta Cryst. (2007). D63, 536-547  [ doi:10.1107/S090744490700964X ]

Structures of and interactions between domains of trigger factor from Thermotoga maritima

E. Martinez-Hackert and W. A. Hendrickson

Synopsis: Crystal structures and cross-linking experiments of the N- and C-terminal domains of T. maritima trigger factor (TF) are presented. Structural and cross-linking data suggest that TF could interact with substrate proteins via hydrophilic surfaces.

PDB references: 2nsa, 2nsb and 2nsc

Online 16 March 2007


short communications


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Acta Cryst. (2007). D63, 548-549  [ doi:10.1107/S0907444907007354 ]

An alternate description of two crystal structures of phospholipase A2 from Bungarus caeruleus

I. Le Trong and R. E. Stenkamp

Synopsis: The noncrystallographic symmetry operations reported for two crystal structures of phospholipase A2 isoforms from the common krait can be reinterpreted as crystallographic operations. The change in space group affects conclusions about the oligomeric forms of the proteins in the crystalline state.

PDB reference: 2osn

Online 16 March 2007


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Acta Cryst. (2007). D63, 550-554  [ doi:10.1107/S0907444907007652 ]

An automated microseed matrix-screening method for protein crystallization

A. D'Arcy, F. Villard and M. Marsh

Synopsis: The formation of nuclei in a crystallization experiment requires the interaction of protein molecules until a critical size of aggregate is created. The formation of such nuclei may be achieved either at very high protein concentrations or at lower levels of saturation with the introduction of seeds to form nucleation sites. Incorporating this seeding step into an automated screening process could have a considerable influence on the number of conditions which produce crystals. Some preliminary results are presented in this article.

Online 16 March 2007


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