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1.  Energetics of 5-bromo-4-chloro-3-indolyl-α-d-mannose binding to the Parkia platycephala seed lectin and its use for MAD phasing 
The first crystal structure of a Mimosoideae lectin, Parkia platycephala has been solved by MAD phasing using 5-bromo-4-chloro-3-indolyl-α-d-mannose as an anomalous X-ray scatterer. This strategy may be useful for structure elucidation of novel lectins or when molecular replacement methods fail.
Parkia platycephala belongs to the most primitive group of Leguminosae plants. Its seed lectin is made up of three homologous β-prism repeats and exhibits binding specificity for mannose/glucose. The properties of the association between the lectin from P. platycephala seeds and monosaccharide ligands were analysed by isothermal titration calorimetry and surface plasmon resonance. The results are consistent with the lectin bearing three thermodynamically identical binding sites for mannose/glucose per monomer with dissociation constants in the millimolar range. Binding of each ligand by the lectin is enthalpically driven. Crystals have been obtained of the lectin in complex with a brominated derivative of mannose (5-bromo-4-chloro-3-indolyl-α-d-mannose), which were suitable for deriving an electron-density map by MAD phasing. In agreement with the thermodynamic data, six Br atoms were found in the asymmetric unit of the monoclinic P21 crystals, which contained two P. platycephala lectin molecules. The availability of other Br derivatives of monosaccharides (glucose, galactose, fucose) may make this strategy widely useful for structure elucidation of novel lectins or when (as in the case of the P. platycephala lectin) molecular-replacement methods fail.
doi:10.1107/S1744309105004835
PMCID: PMC1952276  PMID: 16511032
protein–carbohydrate interactions; Parkia platycephala lectin; isothermal titration calorimetry; surface plasmon resonance; β-prism domain; MAD phasing
2.  Crystallization and preliminary X-ray diffraction analysis of the arginine repressor of the hyperthermophile Thermotoga neapolitana  
The arginine repressor of the hyperthermophile T. neapolitana was crystallized with and without its corepressor arginine. Both crystals diffracted to high resolution and belong to the orthorhombic space group P212121, with similar unit-cell parameters.
The arginine repressor of Thermotoga neapolitana (ArgRTnp) is a member of the family of multifunctional bacterial arginine repressors involved in the regulation of arginine metabolism. This hyperthermophilic repressor shows unique DNA-binding features that distinguish it from its homologues. ArgRTnp exists as a homotrimeric protein that assembles into hexamers at higher protein concentrations and/or in the presence of arginine. ArgRTnp was crystallized with and without its corepressor arginine using the hanging-drop vapour-diffusion method. Crystals of the aporepressor diffracted to a resolution of 2.1 Å and belong to the orthorhombic P212121 space group, with unit-cell parameters a = 117.73, b = 134.15, c = 139.31 Å. Crystals of the repressor in the presence of its corepressor arginine diffracted to a resolution of 2.4 Å and belong to the same space group, with similar unit-cell parameters.
doi:10.1107/S1744309105039618
PMCID: PMC2150929  PMID: 16511254
arginine repressor; regulation of transcription; hyperthermophiles
3.  Expression, crystallization and preliminary X-ray analysis of a ferric binding protein from Thermus thermophilus HB8 
The cloning, expression, purification, crystallization and preliminary X-ray analysis of a ferric binding protein encoded by T. thermophilus HB8 in apo and iron-bound holo states are presented. Four different crystal forms were obtained.
A ferric binding protein from Thermus thermophilus HB8 (TtFbpA) was expressed, purified and crystallized using the hanging-drop vapour-diffusion method. Four different crystal forms were obtained and characterized by X-ray diffraction. Two crystal forms with TtFbpA in the apo state belonged to the orthorhombic space group P212121 (unit-cell parameters a = 42.1, b = 139.3, c = 326.5 Å and a = 42.1, b = 139.3, c = 218.9 Å). The third form with TtFbpA also in the apo state belonged to the monoclinic space group P21 (unit-cell parameters a = 66.5, b = 61.7, c = 73.9 Å, β = 111.7°). The fourth form, with TtFbpA in the iron-bound holo state as confirmed by an atomic absorption spectrophotometry assay, belonged to the trigonal space group P3121 or P3221 (unit-cell parameters a = 63.6, b = 63.6, c = 266.7 Å, α = β = 90.0, γ = 120.0°).
doi:10.1107/S1744309111012929
PMCID: PMC3107153  PMID: 21636922
ferric binding protein; Thermus thermophilus HB8; apo state; iron-bound holo state
4.  Characterization and crystallization of a recombinant IgE Fab fragment in complex with the bovine β-lactoglobulin allergen 
The high-resolution mass-spectrometric characterization, crystallization and X-ray diffraction studies of a recombinant IgE Fab fragment in complex with bovine β-lactoglobulin are reported.
A D1 Fab fragment containing the allergen-binding variable domains of the IgE antibody was characterized by ESI FT–ICR mass spectrometry and crystallized with bovine β-lactoglobulin (BLG) using the hanging-drop vapour-diffusion method at 293 K. X-ray data suitable for structure determination were collected to 2.8 Å resolution using synchrotron radiation. The crystal belonged to the orthorhombic space group P212121, with unit-cell parameters a = 67.0, b = 100.6, c = 168.1 Å. The three-dimensional structure of the D1 Fab fragment–BLG complex will provide the first insight into IgE antibody–allergen interactions at the molecular level.
doi:10.1107/S174430910706160X
PMCID: PMC2373997  PMID: 18097096
antibodies; IgE; food allergens; mass spectrometry
5.  Crystallization of the hydantoin transporter Mhp1 from Microbacterium liquefaciens  
Mhp1, a hydantoin transporter from M. liquefaciens, was purified and crystallized. Diffraction data were collected to 2.85 Å resolution; the crystal belonged to the orthorhombic space group P212121.
The integral membrane protein Mhp1 from Microbacterium liquefaciens transports hydantoins and belongs to the nucleobase:cation symporter 1 family. Mhp1 was successfully purified and crystallized. Initial crystals were obtained using the hanging-drop vapour-diffusion method but diffracted poorly. Optimization of the crystallization conditions resulted in the generation of orthorhombic crystals (space group P212121, unit-cell parameters a = 79.7, b = 101.1, c = 113.8 Å). A complete data set has been collected from a single crystal to a resolution of 2.85 Å with 64 741 independent observations (94% complete) and an R merge of 0.12. Further experimental phasing methods are under way.
doi:10.1107/S1744309108036920
PMCID: PMC2593711  PMID: 19052379
transporters; nucleobase:cation symporter 1 family; membrane proteins; hydantoins
6.  Purification, crystallization and preliminary X-ray diffraction analysis of the thiaminase type II from Staphylococcus aureus  
Crystals of the thiaminase type II from S. aureus are orthorhombic, belonging to space group P212121 with unit-cell parameters a = 103.5, b = 104.1, c = 109.6 Å, and diffracted to 2.6 Å resolution.
Thiaminase type II (TenA) catalyzes the deamination of aminopyrimidines, including the cleavage of thiamine to 4-amino-5-hydroxymethyl-2-methyl­pyrimidine and 5-(2-hydroxyethyl)-4-methylthiazole in the metabolism of thiamine (vitamin B1), in Staphylococcus aureus (Sa). SaTenA was crystallized by the vapour-diffusion method and the resulting crystal diffracted to 2.6 Å resolution usng synchrotron radiation. The crystal is orthorhombic, belonging to space group P212121 with unit-cell parameters a = 103.5, b = 104.1, c = 109.6 Å. With four molecules in the asymmetric unit, the Matthews coefficient is 2.85 Å3 Da−1. Initial attempts to solve the structure by molecular-replacement techniques were successful.
doi:10.1107/S1744309110043174
PMCID: PMC3079971  PMID: 21206023
thiaminase type II; TenA; Staphylococcus aureus
7.  Crystallization and preliminary X-ray diffraction analysis of calexcitin from Loligo pealei: a neuronal protein implicated in learning and memory 
Recombinant squid calexcitin has been crystallized using the hanging-drop vapour-diffusion technique in the orthorhombic space group P212121.
The neuronal protein calexcitin from the long-finned squid Loligo pealei has been expressed in Escherichia coli and purified to homogeneity. Calexcitin is a 22 kDa calcium-binding protein that becomes up-regulated in invertebrates following Pavlovian conditioning and is likely to be involved in signal transduction events associated with learning and memory. Recombinant squid calexcitin has been crystallized using the hanging-drop vapour-diffusion technique in the orthorhombic space group P212121. The unit-cell parameters of a = 46.6, b = 69.2, c = 134.8 Å suggest that the crystals contain two monomers per asymmetric unit and have a solvent content of 49%. This crystal form diffracts X-rays to at least 1.8 Å resolution and yields data of high quality using synchrotron radiation.
doi:10.1107/S1744309105026758
PMCID: PMC1991304  PMID: 16511184
calexcitin; calcium-binding proteins
8.  Production, purification, crystallization and preliminary X-ray structural studies of adeno-associated virus serotype 5 
The production, purification, crystallization and preliminary crystallographic analysis of empty adeno-associated virus serotype 5 capsids are reported.
Adeno-associated virus serotype 5 (AAV5) is under development for gene-therapy applications for the treatment of cystic fibrosis. To elucidate the structural features of AAV5 that control its enhanced transduction of the apical surface of airway epithelia compared with other AAV serotypes, X-ray crystallographic studies of the viral capsid have been initiated. The production, purification, crystallization and preliminary crystallographic analysis of empty AAV5 viral capsids are reported. The crystals diffract X-rays to beyond 3.2 Å resolution using synchrotron radiation and belong to the orthorhombic space group P212121, with unit-cell parameters a = 264.7, b = 447.9, c = 629.7 Å. There is one complete T = 1 viral capsid per asymmetric unit. The orientation and position of the viral capsid in the asymmetric unit have been determined by rotation and translation functions, respectively, and the AAV5 structure determination is in progress.
doi:10.1107/S1744309105028514
PMCID: PMC1991325  PMID: 16511195
adeno-associated virus serotype 5; gene therapy
9.  Crystallization and preliminary X-ray characterization of phosphoglucose isomerase from Mycobacterium tuberculosis H37Rv 
The phosphoglucose isomerase from Mycobacterium tuberculosis H37Rv was crystallized and diffraction data were collected to 2.8 Å resolution.
Phosphoglucose isomerase is a ubiquitous enzyme that catalyzes the isomerization of d-glucopyranose-6-phosphate to d-fructofuranose-6-phosphate. The present investigation reports the expression, purification, crystallization and preliminary crystallographic studies of the phosphoglucose isomerase from Mycobacterium tuberculosis H37Rv, which shares 46% sequence identity with that of its human host. The recombinant protein, which was prepared using an Escherichia coli expression system, was crystallized by the hanging-drop vapour-diffusion method. The crystals diffracted to a resolution of 2.8 Å and belonged to the orthorhombic space group I212121, with unit-cell parameters a = 109.0, b = 119.8, c = 138.9 Å.
doi:10.1107/S1744309107013218
PMCID: PMC2330222  PMID: 17401215
phosphoglucose isomerase; Mycobacterium tuberculosis
10.  Crystallization and preliminary X-ray crystallographic study of phosphoglucose isomerase from Plasmodium falciparum  
Phosphoglucose isomerase from P. falciparum has been crystallized. Diffraction data to 1.8 Å resolution have been collected using synchrotron radiation.
Phosphoglucose isomerase (PGI) is a key enzyme in glycolysis and glycogenesis that catalyses the interconversion of glucose 6-phosphate (G6P) and fructose 6-­phosphate (F6P). For crystallographic studies, PGI from the human malaria parasite Plasmodium falciparum (PfPGI) was overproduced in Escherichia coli, purified and crystallized using the hanging-drop vapour-diffusion method. X-ray diffraction data to 1.5 Å resolution were collected from an orthorhombic crystal form belonging to space group P212121 with unit-cell parameters a = 103.3, b = 104.1, c = 114.6 Å. Structural analysis by molecular replacement is in progress.
doi:10.1107/S1744309110001740
PMCID: PMC2833051  PMID: 20208175
glucose 6-phosphate isomerase; malaria; phosphoglucose isomerase; phosphohexose isomerase
11.  Crystallization and preliminary X-ray crystallographic analysis of a helicase-like domain from a tomato mosaic virus replication protein 
Crystals of the helicase domain from a tomato mosaic virus replication protein obtained using the hanging-drop vapour-diffusion method at 285 K diffracted X-rays to 2.05 Å resolution. They belonged to the orthorhombic space group P212121, with unit-cell parameters a = 85.8, b = 128.3, c = 40.7 Å.
Tomato mosaic virus belongs to the genus Tobamovirus in the alphavirus-like superfamily of positive-strand RNA viruses. The alphavirus-like superfamily includes many plant and animal viruses of agronomical and clinical importance. These viruses encode replication-associated proteins that contain a putative superfamily 1 helicase domain. No three-dimensional structures for this domain have been determined to date. Here, the crystallization and preliminary X-ray diffraction analysis of the 130K helicase domain are reported. Diffraction data were collected and processed to 2.05 and 1.75 Å resolution from native and selenomethionine-labelled crystals, respectively. The crystals belonged to the orthorhombic space group P212121, with unit-cell parameters a = 85.8, b = 128.3, c = 40.7 Å.
doi:10.1107/S174430911104231X
PMCID: PMC3232162  PMID: 22139189
tomato mosaic virus; replicase protein; helicase domain
12.  Crystallization and preliminary X-ray analysis of a novel Kunitz-type kallikrein inhibitor from Bauhinia bauhinioides  
Crystallization and preliminary X-ray diffraction studies are reported for a novel Kunitz-type protease inhibitor from B. bauhinioides which contains no disulfide bridges.
A Kunitz-type protease inhibitor (BbKI) found in Bauhinia bauhinioides seeds has been overexpressed in Escherichia coli and crystallized at 293 K using PEG 4000 as the precipitant. X-ray diffraction data have been collected to 1.87 Å resolution using an in-house X-ray generator. The crystals of the recombinant protein (rBbKI) belong to the orthorhombic space group P212121, with unit-cell parameters a = 46.70, b = 64.14, c = 59.24 Å. Calculation of the Matthews coefficient suggests the presence of one monomer of rBbKI in the asymmetric unit, with a corresponding solvent content of 51% (V M = 2.5 Å3 Da−1). Iodinated crystals were prepared and a derivative data set was also collected at 2.1 Å resolution. Crystals soaked for a few seconds in a cryogenic solution containing 0.5 M NaI were found to be reasonably isomorphous to the native crystals. Furthermore, the presence of iodide anions could be confirmed in the NaI-derivatized crystal. Data sets from native and derivative crystals are being evaluated for use in crystal structure determination by means of the SIRAS (single isomorphous replacement with anomalous scattering) method.
doi:10.1107/S1744309105028496
PMCID: PMC1991323  PMID: 16511193
Kunitz-type kallikrein inhibitors; disulfide bridges; Bauhinia bauhinioides
13.  Crystallization and preliminary crystallographic characterization of the N-terminal Kunitz domain of boophilin 
The N-terminal Kunitz domain of boophilin, a specific thrombin inhibitor, was crystallized. The orthorhombic crystals had an unusually low solvent content and diffracted to beyond 0.87 Å resolution at a synchrotron source.
Boophilin is a tight-binding thrombin inhibitor composed of two canonical Kunitz-type domains in a tandem arrangement. Thrombin-bound boophilin can inhibit a second trypsin-like serine proteinase, most likely through the reactive loop of its N-terminal Kunitz domain. Here, the crystallization and preliminary crystallographic analysis of the isolated N-terminal domain of boophilin is reported. The crystals belonged to the orthorhombic space group P212121 and diffracted to beyond 1.8 Å resolution using a sealed-tube home source and to 0.87 Å resolution at a synchrotron source.
doi:10.1107/S1744309112005532
PMCID: PMC3325814  PMID: 22505414
thrombin inhibitors; noncovalent; blood coagulation; atomic resolution
14.  Cloning, overexpression, purification, crystallization, and preliminary X-ray studies of SP_0149, the substrate binding protein of an ABC transporter from Streptococcus pneumoniae  
The substrate binding protein (SP_0149) of an ABC transporter from Streptococcus pneumoniae was molecularly cloned, overexpressed and purified. Diffraction quality crystals were grown using the hanging-drop vapour-diffusion technique.
A truncated (29 residues from the N-terminus) and N-terminal His-tagged form of SP_0149 from pneumococcal strain ATCC BAA-334 was overexpressed and purified to homogeneity using affinity and gel-filtration chromatography. Diffraction quality crystals were grown at 293 K using the hanging-drop vapour-diffusion technique. X-ray diffraction data were collected to 2.3 Å resolution from a single-crystal that belonged to the orthorhombic space group P212121 with the unit-cell parameters a = 54.56, b = 75.61, c = 75.52 Å. The calculated values of the Matthews coefficient assuming one molecule (with calculated molecular weight of 30 400 Da) in the crystal asymmetric unit and the corresponding solvent content were 2.56 Å3 Da−1 and 52.0%, respectively.
doi:10.1107/S1744309111018422
PMCID: PMC3144799  PMID: 21795797
ABC transporter; Streptococcus pneumoniae; SP_0149; ATCC BAA-334
15.  Crystallization, data collection and phasing of the molybdate-binding protein of the phytopathogen Xanthomonas axonopodis pv. citri  
The molybdate-binding protein (ModA) from X. axonopodis pv. citri was crystallized with sodium molybdate in the presence of PEG or sulfate. The crystal diffracted to a maximum resolution of 1.7 Å and belongs to the orthorhombic space group C2221, with unit-cell parameters a = 68.15, b = 172.14, c = 112.04 Å.
Xanthomonas axonopodis pv. citri ModA protein is the ABC periplasmic binding component responsible for the capture of molybdate. The protein was crystallized with sodium molybdate using the hanging-drop vapour-diffusion method in the presence of PEG or sulfate. X-ray diffraction data were collected to a maximum resolution of 1.7 Å using synchrotron radiation. The crystal belongs to the orthorhombic space group C2221, with unit-cell parameters a = 68.15, b = 172.14, c = 112.04 Å. The crystal structure was solved by molecular-replacement methods and structure refinement is in progress.
doi:10.1107/S1744309106003812
PMCID: PMC2197186  PMID: 16511325
molybdate-binding protein (ModA); Xanthomonas axonopodis pv. citri
16.  Crystallization and preliminary X-ray analysis of an arabinoxylan arabinofuranohydrolase from Bacillus subtilis  
The crystallization and preliminary X-ray analysis of the family 43 glycoside hydrolase arabinoxylan arabinofuranohydrolase from B. subtilis soaked with xylotriose is described in order to gain insight in the way the enzyme binds its substrates.
Arabinoxylan arabinofuranohydrolases (AXH) are α-l-arabinofuranosidases (EC 3.2.1.55) that specifically hydrolyse the glycosidic bond between arabinofuranosyl substituents and xylopyranosyl residues from arabinoxylan, hence their name. In this study, the crystallization and preliminary X-ray analysis of the AXH from Bacillus subtilis, a glycoside hydrolase belonging to family 43, is described. Purified recombinant AXH crystallized in the orthorhombic space group P212121, with unit-cell parameters a = 68.7, b = 73.7, c = 106.5 Å. X-ray diffraction data were collected to a resolution of 1.55 Å.
doi:10.1107/S1744309107033702
PMCID: PMC2335161  PMID: 17671370
arabinoxylan arabinofuranohydrolase; glycoside hydrolase family 43; Bacillus subtilis; substrate binding
17.  Crystallization and preliminary X-ray crystallographic studies of DesR, a thermosensing response regulator in a two-component signalling system from Streptococcus pneumoniae  
The response regulator DesR from S. pneumoniae was cloned, expressed, purified and crystallized. A complete data set was collected to 1.7 Å resolution.
The response regulator DesR, which activates the transcription of the des gene by binding to a regulatory region, is essential for controlling the fluidity of membrane phospholipids. DesR from Streptococcus pneumoniae was overexpressed in Escherichia coli. The protein was purified and crystallized for structural analysis. Diffraction data were collected to 1.7 Å resolution using synchrotron radiation and the crystals belonged to the orthorhombic space group P212121, with unit-cell parameters a = 46.91, b = 71.38, c = 117.73 Å. Assuming the presence of a dimer in the asymmetric unit, this corresponds to a V M of 2.21 Å3 Da−1.
doi:10.1107/S1744309109023082
PMCID: PMC2705646  PMID: 19574651
two-component systems; fatty-acid desaturation; response regulators
18.  Crystallization and preliminary X-ray diffraction of the ZO-binding domain of human occludin 
Crystallization and preliminary X-ray diffraction of the ZO-binding domain of human occludin.
Occludin is a tight-junction protein controlling the integrity of endothelial and epithelial cell layers. It forms complexes with the cytoplasmic proteins ZO-1, ZO-2 and ZO-3. The ZO-binding domain in the C-terminal cytoplasmic region of human occludin has previously been isolated and identified. This domain, as expressed in a bacterial system or isolated from native cellular occludin, maintains its ability to bind ZO-1 and ZO-2. The crystallization conditions of the human ZO-binding domain are reported here. The crystals diffract to 2.3 Å resolution and were shown to belong to the orthorhombic space group P212121, with unit-cell parameters a = 33.3, b = 35.4, c = 107.3 Å.
doi:10.1107/S1744309105007475
PMCID: PMC1952431  PMID: 16511043
occludin; tight junction
19.  Crystallization and preliminary X-ray crystallographic studies of XynX, a family 10 xylanase from Aeromonas punctata ME-1 
XynX, a family 10 xylanase from A. punctata ME-1, was crystallized by the hanging-drop vapour-diffusion method. The crystals diffracted to beyond 1.8 Å resolution.
Xylanases catalyze the hydrolysis of β-1,4-glycosidic linkages within the xylan backbone. XynX is a xylanase from Aeromonas punctata ME-1 and belongs to glycoside hydrolase family 10. While most xylanases show endo-type catalytic activities, XynX shows exo-like catalytic activities, selectively producing xylobiose from birchwood xylan. In this study, XynX was crystallized by the hanging-drop vapour-diffusion method. The crystals belonged to the orthorhombic space group P212121, with unit-cell parameters a = 79.0, b = 88.6, c = 93.2 Å, and diffracted to beyond 1.8 Å resolution.
doi:10.1107/S1744309105002058
PMCID: PMC1952265  PMID: 16511010
Aeromonas punctata ME-1; glycoside hydrolase family 10; xylanases; xylobioses
20.  Crystallization and preliminary X-ray analysis of Streptococcus mutans dextran glucosidase 
Dextran glucosidase from S. mutans was crystallized using the hanging-drop vapour-diffusion method. The crystals diffracted to 2.2 Å resolution.
Dextran glucosidase from Streptococcus mutans is an exo-hydrolase that acts on the nonreducing terminal α-1,6-glucosidic linkage of oligosaccharides and dextran with a high degree of transglucosylation. Based on amino-acid sequence similarity, this enzyme is classified into glycoside hydrolase family 13. Recombinant dextran glucosidase was purified and crystallized by the hanging-drop vapour-diffusion technique using polyethylene glycol 6000 as a precipitant. The crystals belong to the orthorhombic space group P212121, with unit-cell parameters a = 72.72, b = 86.47, c = 104.30 Å. A native data set was collected to 2.2 Å resolution from a single crystal.
doi:10.1107/S174430910703936X
PMCID: PMC2376310  PMID: 17768352
dextran glucosidase; Streptococcus mutans; α-amylase family
21.  Crystallization and preliminary X-ray analysis of βC–S lyases from two oral streptococci 
The βC-S lyases from two oral bacteria, Streptococcus anginosus and S. gordonii, were cloned, overproduced, purified and crystallized. The obtained crystals were characterized by X-ray diffraction.
Hydrogen sulfide, which causes oral malodour, is generally produced from l-­cysteine by the action of βC–S lyase from oral bacteria. The βC–S lyases from two oral bacteria, Streptococcus anginosus and S. gordonii, have been cloned, overproduced, purified and crystallized. X-ray diffraction data were collected from the two types of crystals using synchrotron radiation. The crystal of S. anginosus βC–S lyase belonged to the orthorhombic space group P212121, with unit-cell parameters a = 67.0, b = 111.1, c = 216.4 Å, and the crystal of S. gordonii βC–S lyase belonged to the same space group, with unit-cell parameters a = 58.0, b = 73.9. c = 187.6 Å. The structures of the βC–S lyases were solved by molecular-replacement techniques.
doi:10.1107/S1744309109030371
PMCID: PMC2795589  PMID: 19724121
βC–S lyases; Streptococcus anginosus; Streptococcus gordonii
22.  Exploration of triple-helical fragments: crystallization and preliminary X-ray diffraction of d(TGGCCTTAAGG) 
The crystallization and X-ray data collection of the undecamer d(TGGCCTTAAGG) are reported.
The nonamer d(GCGAATTCG) and decamer d(GGCCAATTGG), containing one and two overhanging guanines, respectively, form G·GC triplets in their crystal packing. In order to introduce a third subsequent T·AT triplet, the decamer was further extended by one overhanging thymine residue. Two different crystal morphologies of the sequence d(TGGCCTTAAGG) were obtained by hanging-drop vapour diffusion and diffracted to 2.5 and 2.3 Å resolution, respectively. However, both crystals belong to the orthorhombic space group P212121, with similar unit-cell parameters. Therefore, the two data sets could be merged to a resolution of 2.4 Å with unit-cell parameters a = 26.97, b = 41.12, c = 52.72 Å.
doi:10.1107/S1744309106054522
PMCID: PMC2330110  PMID: 17183175
triple helix; triplet; Hoogsteen; reverse Hoogsteen
23.  Crystallization and preliminary X-ray diffraction studies of a protein disulfide oxidoreductase from Aeropyrum pernix K1 
A protein disulfide oxidoreductase from A. pernix K1 has been crystallized for the first time. The crystals belong to space group I222 or I212121 and diffract to 1.93 Å resolution.
A protein disulfide oxidoreductase from the archaeon Aeropyrum pernix K1 has been overexpressed in Escherichia coli and crystallized at 298 K using the hanging-drop vapour-diffusion method. Crystals belong to the space group I222 or I212121, with unit-cell parameters a = 90.59, b = 102.43, c = 128.96 Å. A complete data set has been collected at the Elettra synchrotron source in Trieste to 1.93 Å resolution using a single frozen crystal.
doi:10.1107/S1744309105004057
PMCID: PMC1952279  PMID: 16511034
protein disulfide oxidoreductases
24.  Crystallization and preliminary crystallographic analysis of recombinant immunoglobulin G-binding protein from Streptococcus suis  
Crystallization of recombinant IgG-binding protein expressed in Escherichia coli using the hanging-drop vapour-diffusion method is described. The crystals belonged to space group P212121, with unit-cell parameters a = 38.98, b = 43.94, c = 78.17 Å.
Streptococcus suis, an important zoonotic pathogen, expresses immunoglobulin G-binding protein, which is thought to be helpful to the organism in eluding the host defence system. Recombinant IgG-binding protein expressed in Escherichia coli has been crystallized using the hanging-drop vapour-diffusion method. The crystals belonged to space group P212121, with unit-cell parameters a = 38.98, b = 43.94, c = 78.17 Å and one molecule in the asymmetric unit. Diffraction data were collected to 2.60 Å resolution.
doi:10.1107/S1744309108020149
PMCID: PMC2494965  PMID: 18678951
Streptococcus suis; immunoglobulin G-binding protein
25.  Purification, crystallization and preliminary X-ray crystallographic analysis of rice Bowman–Birk inhibitor from Oryza sativa  
Rice Bowman–Birk inhibitor was expressed and crystallized.
Bowman–Birk inhibitors (BBIs) are cysteine-rich proteins with inhibitory activity against proteases that are widely distributed in monocot and dicot species. The expression of rice BBI from Oryza sativa is up-regulated and induced by pathogens or insects during germination of rice seeds. The rice BBI (RBTI) of molecular weight 15 kDa has been crystallized using the hanging-drop vapour-diffusion method. According to the diffraction of rice BBI crystals at a resolution of 2.07 Å, the unit cell belongs to space group P212121, with unit-cell parameters a = 74.37, b = 96.69, c = 100.36 Å. Preliminary analysis indicates four BBI molecules in an asymmetric unit, with a solvent content of 58.29%.
doi:10.1107/S1744309106014795
PMCID: PMC2243081  PMID: 16754971
Bowman–Birk inhibitors; rice

Results 1-25 (244214)